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Heinrichs1994Hendriks1996 6Hendriks1998Z Herper1998® Higgins1995 Hilder19909 Hilder19909 Hilder19909 Hilder19909L Hilder19909[ Hilder1990K Hilder19919J Hilder19929\ Hilder1993˜ Hilder19939¶ Hilder19931° Hilder19949s Hill19933C Hines1993G Hodges19879½ Honee1994Z Hopkins1998] Hoshizaki1994^ Houk1986VK Howe1991± Huang1994‰ Huesing1990_ Huesing1991` Huesing1991a Huesing1991b Huesing1991V Huesing2000Hulscher1996 c Hwang1978d Hypsa1995< Ilett2001 Isaac1994rIshikawa19944eJacquard1977xf JaffŽ1992g Janzen1976h Janzen1986Jennings19949i Jermy1993j Jiang1995ª Jouanin1995k Jouanin1998l Journy1991g Juster1976• Kabat1979s Kadwell1993 Kaiser20010| Kamita19919‚ Kamita19919m Kanost1991±Karnosky1994xn Kawabe1980 Kawabe19811m Kawooya1991oKeinanen1994p Kennedy1976} Kerlan1984Ê Kim1992$ Klinkhamer1995q Knowles1986r Kobayashi1994o Kohr19941 Kok1996 Koninkx19966 Koninkx1998s Koziel1993Ê Kumar1992t Kumar1993¨ Kumar1994u Kyriakides1994s L.1993w Laing1994" Lang19909o Laukkanen1994s Launis19933m Law1991 Le Boulc'h1993¦ Lee1993* Leitch20002É Lemos1989v Lepier1994 Levine19949s Lewis1993h Liener1986w Liener1986“ Liljegren19882 Lindquist1994x Lis1986y Lis1986 Lun1995z Luo1997j Luthe1995{ Mac Gaughey1986| Maccutchen1991É Macedo19898| Maddox19919‚ Maddox19919s Maddox19933| Maeda1991‚ Maeda1991 Main19949º Main19949} Maison1984€ Maison19844 Maris19993Martinez-Ramirez1994œ~Martinez-Ramirez1994À Masson1995z Masson19979}Massonie1984x€Massonie1984Å Maudlin1994 Mazza1995z Mazza1997 McCall1995‚ McCutchen1991 Mcgregor1994xƒMckenzie1995xº McManus1994s McPherson1993„ Meeusen1989s Meghji19939G Meik19878ÊMenancio-Hautea1992s Merlin19939‘ Mesterhazy1993… Milner1994† Milner1994L Minney19909ÅMolyneux1994x€ Monet1984‡ Monties1981® Moore1995Á Moran1995¶ Morhy1993k Morrot1998iˆ Mourey19976 Mourey1998W Mullins1995½ Munsterman19949‰ Murdock1990` Murdock1991a Murdock1991b Murdock1991Ï Nardon20044ŠNarvaez-Vasquez1992‹ Natori1990Œ Natori1994Ä Nault1996t Neet19933 Newby1980‰ Nielsen1990à Nobel1995p Oatman19766oOkerblom19944ŽOllivier1981xŠOrozco-Cardenas1992 Osborn1988t Owen19933' Pages1994| Palekar1991‚ Palekar1991 Papp1990‘ Papp1993’ Pathak1993h Pearce1986“ Pearce19881 Pearson1994ˆPedelacq1997x” Pennacchio1995• Pereira1979É Peres Silva1989© Perring1993œ Peumans1990t Peumans1993› Peumans1993M Peumans1995– Peumans1995¤ Peumans1995 Peumans1996­ Peumans1996 Pham-Delgue2001 Pham-Delgue2001# Pickett1987¾ Piron1995' Pitrat19949± Podila1994 Podoler1970 Poppy2001 Poppy2001J Powel1992\ Powell19939— Powell1993˜ Powell1993° Powell1994M Powell19959™ Powell1998‰ Pratt1990WPrivalle1995 Purcell1994F Pusztai1984G Pusztai1987N Pusztai1989œ Pusztai1990š Pusztai1991› Pusztai1993 Pusztai19966 Puzo19981ž R&I1994* Raemaekers2000Ÿ Raes1994 ¢ RahbŽ1990£ RahbŽ1992« RahbŽ1993¬ RahbŽ1994¤ RahbŽ1995ª RahbŽ1995 RahbŽ1996­ RahbŽ1996  RahbŽ1998¡ RahbŽ1998Î RahbŽ2004Ï RahbŽ2004 Raikhel1991¦ Raikhel1993¥ Raikhel1994t Rao1993§ Rao1994¨ Rao19943 Real1994R~ Real19941© Reuter1993s Rhodes19939¶ Richardson1993Í6 Riviere1998Roitberg19956 Rouge1998ˆ RougŽ1997œ Rubio1990h Ryan19868“ Ryan19888m Ryan19919Š Ryan1992r Sabnis19898ˆ Samama199796 Samama19989ASandeman1994z Sangadala1997« Sauvion1993¬ Sauvion1994¤ Sauvion1995ª Sauvion1995 Sauvion1996­ Sauvion1996Î Sauvion2004Ï Sauvion2004® Schroeder1995A Seaton1994o Seeburg1994f Seidl1992B Serdy1993NShackley19899‰ Shade1990` Shade1991a Shade1991b Shade1991ÊShanmugasundarum1992À Shapiro1994x Sharon1986y Sharon1986Sheppard1994J¯ Shewry1991° Shi1994± Shin1994² Shufran19963 Silva1994³ Simpson1994@ Sims19922´ Singer1986µ Singh1986j Siregar1995¶ Sousa1993u Spence19944™ Spence1998® Spencer1995 Stevens1994› Stewart1993½Stiekema199498 Stirpe19919· Stoger1999¸ Storer1995¹ Summerfield1993 Sun1988º Sutherland1994Í» Tabashnik1995® Tabe19955 Tadmor19709Ê Talekar19921 Tellam19944> Thi Loc2000t Timm19933¼ Tjallingii1987Tompkins1994J© Toscano1993”Tremblay199590 Trumble1994œ Van Damme1990› Van Damme1993° Van Damme1994M van Damme1995 van Damme1996­ van Damme1996$van der Meijden1995½ van der Salm1994 Q van Driessche1993¸ van Emden1995m van Heusden1991–Vandamme1995Ÿ Verbeke1994½ Visser19949¾ Visser1995¿ Visser1995À Volkov1995| Volrath1991‚ Volrath1991Á Vondohlen19951 Vuocolo1994# Wadhams1987 Wallace1974° Wang1994à Wang1995`„ Warren19899s Warren19939Ä Wayadande1996& Wehner19911Å Welburn1994v Wieczorek1994Æ Wilkinson1995j Willeford1995Williams1992xjWilliams19955·Williams1999xÇ Wiseman1995$ Wolff1995#Woodcock19877* Woodhouse2000= Woodhouse2001s Wright19939É Xavierfilho1989È Xavierfilho1991¿ Yan1995c Yang19788Ê Young1992m Ziegler1991S Zilberberg1990ÍË Zilberberg1991Ì Zilberberg1992S Zlotkin1990Ë Zlotkin1991Ì Zlotkin1992Í Zlotkin1993m van Heusden1991| Volrath19911 Vuocolo1994# Wadhams1987s Warren19939& Wehner19911v Wieczorek1994j Willeford1995Williams1992xjWilliams19955$ Wolff1995#Woodcock19877* Woodhouse2000= Woodhouse2001s Wright19939c Yang19788m Ziegler1991S Zilberberg1990ÍS Zlotkin1990enet !"%'()ant cottonf_insecte, rŽsistance, cotton genie genetique, transgenose, Chitinas, lectine, Bt, revue, insectenFuchs, M. Gonsalves, D.é 1995º´Resistance of transgenic hybrid squash ZW-20 expressing the coat protein genes of zucchini yellow mosaic virus and watermelon mosaic virus 2 to mixed infections by both potyvirusesBio/Technology 2+345 Park Ave South, New York, NY 10010-1707 Nature Publishing Co13 1466-1473 Bio/ Authors¿Journals WKeywords ?                               ÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿ*„ ”æ(Ed.), COSTES C.l8353, Society for Experimental Biology Seminar SeriesϘ Adams, J.R.( Adams, M.E.( Adang, M.J.( Albrecht, A.(Alexander, D.C.¦l Altabella, T. Ando, Y.à Antunes, R.V.Applebaum, S.W.¦l Arcus, Y.M.( Ary, M.B. Azuma, M. Backus, E.A.( Bakker, P.(Balasubramaniam, N.K. Barbieri, L.( Bardocz, S.(Bardocz, S., Pusztai, A.– Bastard, Y.( Batterham, P. Bedoyan, J.K. BEHNKE, H.D., SJOLUND, R.D.üT Beland, G.L.( Bell, H.A.(Berberich, S.A.¦l Bernays, E.A. Bharathi, M.( Biggs, D.R.( Bliss, F.A.(BonadŽ Bottino, M.›”BonadŽ-Bottino, M.›” Bondari, K.( Bordat, D.( Bosch, D. Boulter, D.(Bournoville, R.¦l Bowman, C.( Brabant, P.( Brehelin, M.(Broekaert, W.F.¦l Brousseau, R. Brown, D.S.( Brown, S.M.( Bryden, J.(Burgess, E.P.J.¦l But™t, R.P.T. Cadogan, L.C. Caillaud, M.(Calatayud, P.A.¦lcallahan, F.E.Цl Cameron, M.M.Campos, F.A.P.Цl Cardona, C.( Carlini, C.R.Carozzi, N., Koziel, M.›– Carozzi, N.B. Carrire, Y.(Carvalho, M.M.Цl Casey, M.L.( Casida, J.E.( Causse, H.( Chapman, R.F. Charles, H.( Chekkafi, A.( Chen, J.Q.( Chino, M.Choudary, P.V.ЦlChrispeels, M.J.lChristeller, J.T. Christou, P.( Clark, S.J.(Coelho, L.C.B.B.l Cohen, E. Cole, R.A.( Couty, A. Craig, S. Crenshaw, R.(Crenshaw, R.W.Цl Cronshaw, J.( Czapla, T.C.( Czapla, T.H.( Danesh, D.( davis, F.M.( Dawson, G.W.( Dawson, J.(de Jager, C.M.Цl de Jong, T.J.de la Vina, G.Цlde Ponti, O.M.B.lDelaunay, A.M.Цl Delobel, B.( Desai, N. Dewey, F.M.(Dhillon, N.P.S.¦l Digilio, M.C. Dobie, P. Dogimont, C.(Donaldson, R.A.¦lDorschner, K.W.¦l Douglas, A.E. Dove, J.à Down, R.E.( Drif, L.à Driouich, A.( Edmonds, H.S.4/Eds D'Mello, J.P.F.; Duffus C.M. & Duffus, J.H.83Eds van der Poel, A.F.B.; Huisman, J. & Saini, H.S.Ϙ Edwards, G.A. Edwards, J.P. Ehler, L.E.HEigenbrode, S.D.lEisemann, C.H.Цl Ellar, D.J.(,(Emden, Thomas A. Miller & Helmut S. van Erb, W.A. Escriche, B.( Estada, U.( Etzler, M.E.( Evola, S.V.( Ewen, S.W.B.( Fabre, C. Faye, L.à Febvay, G.( Feng, L.X.( Fenton, K.A.( Ferrari, C.( Ferre, J. FerrŽ, J. Fitches, E.( Fitches, E.C.Fitchette-Laine, A.C.Flemming, J.E.ЦlFlickinger, N.J.l Foard, D.E.( Foissac, X.( Ford, L.à Fowler, E.( Fritz, R.S.( Fry, K.L. Fuchs, R.L.HFukumorita, T.Цl Furk, C.àGatehouse, A.M.RlGatehouse, A.M.R.Gatehouse, J.A.¦lGatehouse, L.N.¦l Giband, M.( Girard, C.( Girousse, C.( Gollasch, S.( Gomord, V.(Gonzalez-Nebauer, S.” Goode, J.A.( Grant, G. Greene, R.HGreenplate, J.T.lGreenway, R.M.ЦlGriffiths, D.C.¦lGroeters, F.R.ЦlGrubhoffer, L.Цl Gruezo, F.( Guez, M.àGuimaraes, J.A.¦l Gurevitz, M.( Haack, R.A.( Habibi, J.(Hamilton, W.D.O.l Hammock, B.( Hardie, D.C.( Hardy, J.L.( Harper, S.M.H Harvey, W.R.(Heinrichs, E.A.¦l Hendriks, H.( Herper, S.M.(Higgins, T.J.V.¦l Hilder, V.A.( Hill, M.à Hines, C.M.( Hodges, R.J.( Honee, G. Hopkins, T.L. Hoshizaki, S. Houk, E.J.H Howe, D.S.( Huang, Y.H.( Huesing, J.E. Hulscher, S.( Hwang, D.L.H Hypsa, V. Ilett, C. Isaac, B.G.( Ishikawa, H.( Jacquard, A.H JaffŽ, W.G.H Janzen, D.H.HJennings, M.G.Цl Jermy, T. Jiang, B. Jouanin, L.( Journy, N.( Juster, H.B.( Kabat, E.A.( Kadwell, S.( Kaiser, L.( Kamita, S.G.( Kanost, M.R.(Karnosky, D.F.Цl Kawabe, S.( Kawooya, J.K. Keinanen, K.( Kennedy, G.G. Kerlan, C.( Kim, D.H.Klinkhamer, P.G.L.›” Knowles, B.H. Kobayashi, M. Kohr, G.à Kok, W.Îà Koninkx, J.( Koziel, M.G.( Kumar, L. Kumar, M.A.HKyriakides, T.R.l L., Crossland,)LABEYRIE V., FABRES G., LACHAISE D. (Eds) Laing, W.A.( Lang, B.A.(  ÐWAdv. Insect Physiol.@;Agr. Ecosyst. Environ. Agriculture Ecosystems & Environment9 Anim Behav Animal Behavioure0*Ann. Appl. Biol. Annals of Applied Biology Ann. Bot.Annu. Rev. Entomol.ÐlhAnnu. Rev. Plant Physiol. Plant Mol. Biol. Annual Review of Plant Physiology and Plant Molecular BiologyD>Appl Biochem Biotechnol Applied Biochemistry and Biotechnology |€D@Appl. Environ. Microbiol. Applied and Environmental Microbiology€D>Arch. Biochem. Biophys. rchives of Biochemistry and Biophysics |€PMArch. Insect Biochem. Physiol. Archives of Insect Biochemiqtry and PhysiologyTNArch. Insect. Biochem. Physiol. Archives of Insect Biochemistry and Physiology= Bio/Technology Bio/TechnologyXRBiochem. Biophys. Res. Commun. Biochemical and Biophysical Research CommunicationsBiochem. J. Biochem. J.K85Biochem. Soc. Trans. Biochemical Society TransactionsD>Bioelectrochem Bioenerg. Bioelectrochemistry and Bioenergetics |€$Biotechnology Bio - Technology |€,)Br. J. Nutr. British Journal of Nutrition0-Bul. Entomol. Bulletin Entomological researchBull. OEPP Bull. OEPPhbCan. J. Forest Res. Canadian Journal of Forest Research - Revue Canadienne de Recherche Forestiere41Cell and Tissue Research Cell and Tissue ResearchComp. Biochem. Physiol.KXRComp. Biochem. Physiol. [A] Comparative Biochemistry and Physiology A - PhysiologyWÐ`$Crop Protection Crop Protection|€ Crop Science Digestion($Ecol. Entomol. Ecological Entomology Endeavour EndeavourÐ@;Entomol. exp. appl. Entomologia experimentalis et applicata (%Entomol. Fennica Entomologica Fennica0*Environ. Entomol. Environmental Entomology Euphytica FEBS Letters("Fla. Entomol. Florida EntomologistWÐ Heredityp$!Histochem J Histochemical Journal InfoZooüT Insect Biochem. Mol. Biol.×LGInsect. Biochem. Molec. Biol. Insect Biochemistry and Molecular Biology;p<9Int. J. Parasitol. International Journal for Parasitology0*J Exp Biol Journal of Experimental Biology83J. Agr. Entomol. Journal of Agricultural Entomology|€J. agric. Food Chem.4/J. Appl. Entomol. Journal of Applied Entomology|€4.J. Biol. Chem. Journal of Biological Chemistry |€ J. Cell. Sci. J. chem. Ecol. J. chem. Ecol.40J. econ. Entomol. Journal of Economic Entomology€0+J. Exp. Bot. Journal of Experimental Botanyi€0+J. Insect Behav. Journal of Insect BehaviorJ. Insect Physiol.Ð<7J. Invertebr. Pathol. Journal of Invertebrate Pathologyи0,J. Mol. Evol. Journal of Molecular Evolution,'J. Sci. Food Agric. J. Sci. Food Agric.|€ Journal of Chemical Ecologye<9Journal of Insect Physiology Journal of Insect PhysiologyKoren J. Appl. Entomol.K84Med. Vet. Entomol. Medical and Veterinary Entomology€Mem. Inst. Oswaldo CruzK(%Molecular Breeding Molecular Breeding non publiŽ,'Nutr. Biochem. Nutritional Biochemistry|€Outlook on AgricultureK(#Parasitol. Today Parasitology TodayÐ Pestic. Biochem. Physiol.$Pestic. Sci. Pesticides ScienceÒ Phytochemistry Phytochemistry Phytoma;p Plant CellPlant Cell Physiol.Ð,&Plant Gene Transf. Plant Gene Transfer |€Plant Physiol.–xPlant Sci. Plant Science,)Plant. Mol. Biol. Plant Molecular Biology Planta;pLHProt. Struct. Func. and Gen. PROTEINS: Structure, Function, and Geneticsp Res. Immunol.Science Science–xTheor. Appl. Genet.Ð$Tissue and Cell Tissue and Cell|€Tissue Cell Tissue & Cell Toxicon;p41Trend Ecol. Evolut. Trends in Ecology & Evolution,(Trop. Pest Man. Tropical Pest Management€x  Ì<¤ž$lectin, mode d'action, mannose, inhibition de croissance, Myzus persicae, insecte, binding, milieu artificial, toxicite, modelisation, rm, NPA, GNA, ASA, RSA-€$lectine, insecte $lutbio, aphididae, homoptera¨£$nic, $TOXPROT, Lectine, Inhibiteur protease, Genie genetique, Revue, RŽsistance, Transgenose, Lepidoptera, Orthoptera, Coleoptera, Homoptera, WGA, insecte, plante 0¼¶$nic, Fabaceae, Phaseolus vulgaris, Lectine, $TOXPROT, Toxicite, Binding, Intestin, Graine, Histopathologie, Coleoptera, Bruchidae, Callosobruchus maculatus, RPI, RŽsistance, insecteWÌ”$phloem, Homoptera, Aphididae, Acyrthosiphon pisum, Medicago sativa, rŽsistance, insecte, antibiose, stylectomie, amino acides, sucre, exudationž $toxprotp@<$TOXPROT, insecte, lectine, inhibiteur protease, transgenosePK$TOXPROT, Lectine, Brevet, Cysteine, Sequence, Pontage, insecte, rŽsistance(xs$TOXPROT, Lectine, Coleoptera, Developpement larvaire, Bruchidae, Callosobruchus maculatus, Toxicite, HPLC, insectehb$toxprot, lectine, Con A, GNA, mode d'action, revue, biologie molŽculaire, reconnaissance, insecteWϘ¨¢$toxprot, lectine, mode d'action, phytohemagglutinin, PHA, castor bean, Ricinus communis, ricin, jeriquinty, Abrus precatorus, plante, binding, recepteur, insecte 0TO$toxprot, lectine, rŽsistance, insecte, transgenose, tabac, inhibiteur protease²0À»$TOXPROT, Lectine, Urtica dioica, Oryza sativa, Poaceae, Coleoptera, Bruchidae, Callosobruchus maculatus, Amylase, Inhibiteur protease, Croissance, Toxicite, RŽsistance, RPI, WGA, insecteÍp ›$toxprot, mode d'action, intestin , rat, Triticum aestivum (WGA), thorn apple (Datura stramonium), nettle (Urtica dioica), mode d'action, binding, lectine,ý$toxprot, plant lectin, insecte, rŽsistance, milieu artificiel, Callosobruchus maculatus, cowpea weevil, osage orange lectin, peanut agglutinin, N-acetylgalactosamine, GalNAc, N-acetylglucosamine,GlcNAc, wheat germ (WGA), rice (RL), tomato (TL), jimson 84$toxprot, revue, lectine, insecte, Con A, gŽnŽralitŽ0xt$toxprot, revue, UDA, chitinase, heveine, chitin-binding protein, chitine, transgenose, insecte, rŽsistance, plante,0lh$TOXPROT, RPI, RŽsistance, Fabaceae, Coleoptera, Bruchidae, Revue, insecte, lectine, inhibiteur proteaseÀ $TOXPROT, Test biologique, Toxicite, Proteine, Homoptera, Aphididae, Acyrthosiphon pisum, Lectine, insecte, rŽsistance, plante, milieu artificiel, LC50, DL50PJ$TOXPROT, Toxine, Sequence, Specificite, Scorpionidae, Neurotoxicite, ADNc;pda$toxprot, transgenose, insecte, rŽsistance, CpTI, IP, inhibiteur protease, revue, plante, lectine˜•$TOXPROT, Vigna unguiculata, Coleoptera, RPI, RŽsistance, Inhibiteur protease, Bruchidae, Callosobruchus maculatus, Amylase, Lectine, Tannin, insecte , lectine,HON A-CHAIND ABRIN-AECACTION-POTENTIALSACTIVE-TRANSPORTPAcyrthosiphon pisum ACYRTHOSIPHON-PISUMINPKADNc, Sequence, $TOXPROT, Neurotoxicite, Insecta, Scorpionidae, Specificite(#Affinity Chromatographie d'affinitŽ agglutination AgglutininmmuAGROBACTERIUM RHIZOGENESAlataALPHA-AMYLASE-INHIBITORRAAmblysellus grexf Amino AcidscaAMINO-ACID RECEPTORSAMINO-ACID-SEQUENCE  œAminoacide, Phloeme, Saccharose, $PHLOEM, Stylectomie, Homoptera, Cicadellidae, Oryza sativa, Poaceae, pH, Potassium, Mineral, Pression osmotique, Laser YAG\YAminopeptidase, Bacillus thuringiensis, Toxine, Recepteur, Lectine, N-acetylgalactosamineantibacterial defenseANTIBACTERIAL PROTEINSectANTIFUNGAL PROPERTIESliAntimetabolic proteins, plante, rŽsistance, corn rootworms, Diabrotica sp., $toxprot, lectine, insecte,$antimony silver/silver chlorideÔ  Antinutritif  antixenoseiosAPHELINIDAE HYMENOPTERAEPAPHID Aphididae AphidiinaeKAphis gossypiiidiAphis-Gossypii! Apis Mellifera (L)s ŒˆAprotinine, Inhibiteur protease, Brevet, $TOXPROT, Synergie, Lectine, WGA, Ostrinia nubilalis, Lepidoptera, Bowman-Birk, insecte, brevetàArachis hypogaeaiXUArcelin, Cristallisation, Lectine, Phaseolus vulgaris, Glycoproteine, Spectroscopie X !!!!!!!!!!!!!""""""""""""""%%%%%%%%%'''''''''(((((())))))))""ôR  œ,  n ” Þ,R†ÈZ–<5Adams, J.R. Sheppard, C.A. Shapiro, M. Tompkins, G.J. 1994 šLight and electron microscopic investigations on the histopathology of the midgut of gypsy moth larvae infected with LdMNPV plus a fluorescent brightener.J. Invertebr. Pathol.(!Journal of Invertebrate PathologyV642–156-159Ni 0181ÖèâLymantria dispar nuclear polyhedrosis virus; fluorescent brightener; histopathology; electronique microscopie , MET; immunocytochimie; NUCLEAR POLYHEDROSIS-VIRUS; OPTICAL BRIGHTENERS; LEPIDOPTERA; BACULOVIRUSES; HOSTS, midgut,VPNote JR Adams, USDA ARS, Insect Biocontrol Lab, Barc-W, Beltsville, MD 20705 USA Albrecht, A. 1994Entomol. FennicaEntomologica Fennica52105-113Ni 0177"collection, insecte, aphiderkArticle A Albrecht, Univ Helsinki, Finnish Museum Nat Hist, Zool Museum, POB 17, SF-00014 Helsinki, FinlandoLEFreeze-drying techniques for preserving aphids (Homoptera: Aphidodea)o$Altabella, T. Chrispeels, M.J. 1990Plant Physiol.932805-810º 2092ÖiTobacco plants transformed with the bean aai-gene express an inhibitor of insect a-amylase in their seedsi ) * Q R †€Solanaceae, Proteine, Inhibiteur protease, Transgenose, Amylase, Graine, RPI, Coleoptera, RŽsistance, Lectine, $TOXPROT, insecte$Antunes, R.V. Coelho, L.C.B.B. 1994‚|Identification of lectin activity in the hemolymph of castnia licus drury, a Sugar-Cane giant borer (Lepidoptera-Castniidae)Appl Biochem Biotechnolö,&Applied Biochemistry and Biotechnology 60999 Riverview Drive, Suite 208, Totowa, NJ 07012 Humana Press Inc471f 33-37d 0273-2289 <6Lectin; Castnia Licus; PURIFICATION; ISOLECTINS; SEEDSHBCastnia licus Drury, in the larvae stage, is a major pest in the sugarcane industry of Northeastern Brazil (giant borer). A natural hemagglutination activity was detected in the larvae hemolymph of this insect and the activity have not been inhibited by tested carbohydrates. Fractionation with ammonium sulfate showed that the supernatant of the 15-30% fraction (S15-30%) had the lectin's highest specific activity. Acidic and basic lectin activities were separated by chromatography on CM-cellulose; the fractionated molecular forms showed distinct electrophoresis mobilities.Ž‡Article LCBB Coelho, Univ Fed Pernambuco, Ctr Ciencias Biol, Dept Bioquim, AV Moraes Rego S-N, Cidade Univ, BR-50730 Recife, PE, Brazil ,&Applebaum, S.W. Tadmor, U. Podoler, H. 197013 61-70 1132¡The effect of starch and a heteropolysaccharide fraction from Phaseolus vulgaris on development and fecundity of Callosobruchus chinensis (Coleoptera: Bruchidae)1 > P q ‰ d]Coleoptera, Bruchidae, Heteroside, Fabaceae, Phaseolus vulgaris, RŽsistance, Lectine, insecte.'Entomologia experimentalis et applicataEntomol. exp. appl.eApplebaum, S.W. Guez, M. 197215203-207n 1131ƒComparative resistance of Phaseolus vulgaris beans to Callosobruchus chinensis and Acanthoscelides obtectus (Coleoptera: Bruchidae)o  , 6 N S k d]Coleoptera, Bruchidae, Heteroside, Fabaceae, Phaseolus vulgaris, RŽsistance, Lectine, insecte.'Entomologia experimentalis et applicataEntomol. exp. appl.ef_Bell, H.A. Fitches, E.C. Down, R.E. Maris, G.C. Edwards, J.P. Gatehouse, J.A. Gatehouse, A.M.R. 1999BÕThe effect of snowdrop lectin (GNA) delivered via artificial diet and transgenic plants on Eulophus pennicornis (Hymenoptera: Eulophidae) a parasitoid of the tomato moth Lacanobia oleracea (Lepidoptera: Noctuidea)Œ [ o ª ¼ "Journal of Insect Physiology45983-991 "Journal of Insect Physiology Nic›0Ãsnowdrop lectin, GNA, artificial diet, transgenic plant, Eulophus pennicornis, Hymenoptera, Eulophidae, parasitoid, tomato moth, Lacanobia oleracea, Lepidoptera, Noctuidea, mode d'action, lectineº 9 M  “  JIPŒ"Bernays, E.A. Chapman, R.F.r 1994Effects of experienceÝ .'Thomas A. Miller & Helmut S. van Emdenn4-Host-plant selection by phytophagous insects. New York-London Chapman & Hall206-229@Ni 0057:4insecte, comportement, revue, puceron, test de choix0)Biggs, D.R. Greenway, R.M. Mcgregor, P.G. 1994731 31-37Ni 0211ºb[micro electrode; pH; antimony silver/silver chloride; redox; gut contents; SOIL, midgut, pHmleArticle DR Biggs, Agres Grasslands, Genet Molec Lab, Private Bag 11008, Palmerston North, New Zealandb[An antimony-silver/silver chloride electrode system for measuring pH in insect gut contents.'Entomologia experimentalis et applicataEntomol. exp. appl.eBonadŽ Bottino, M. 1993œ–DŽfense du colza contre les insectes phytophages dŽprŽdateurs : Žtude d'une stratŽgie basŽe sur l'expression d'inhibiteurs de protŽases dans la plante Paris-Sud , Centre d'Orsay 155Thse 3me cycleNi 0239hainsectes, transgenese, inhibiteur de proteases, coleopteres, lectines, revue, plante transgŽniquesthese complete chez YvanNHBoulter, D. Edwards, G.A. Gatehouse, A.M.R. Gatehouse, J.A. Hilder, V.A. 1990Crop ProtectionCrop Protection9351-354‚ 4278rkAdditive protective effects of different plant-derived insect resistance genes in transgenic tobacco plantsVO$toxprot, lectine, rŽsistance, insecte, transgenose, tabac, inhibiteur protease0*Boulter, D. Gatehouse, A.M.R. Hilder, V.A. 1990Plant Gene Transf.Plant Gene Transfer 129267-273B<$TOXPROT, insecte, lectine, inhibiteur protease, transgenose4DLEEngineering enhanced natural resistance to insect pests: a case studyD0*Boulter, D. Gatehouse, A.M.R. Hilder, V.A. 1990:3Genetic engeneering of plants for insect resistancei255-266n Versailles 4-6/12/90Congres 2039voRevue, Genie genetique, RPI, RŽsistance, Lectine, Inhibiteur protease, Bacillus thuringiensis, Toxine, $TOXPROT9@:Boulter, D. Gatehouse, J.A. Gatehouse, A.M.R. Hilder, V.A. 1990 Endeavour Endeavour14185-190 21964D:3Genetic engineering of plants for insect resistanceDÎÇRevue, Transgenose, RŽsistance, Proteine, Inhibiteur protease, Bacillus thuringiensis, Vigna unguiculata, Lutte varietale, Genie genetique, $TOXPROT, lectine, gŽnŽralitŽ, insecte, inhibiteur proteaseD Boulter, D.ÿ 1993Phytochemistry346 1453-1466Phytochemistry 4280LEtransgenose, revue, insecte, resitance, inhibiteur protease, lectine,VNHInsect pest control by copying nature using genetically engineered cropsBournoville, R.ÿ 1980 Bull. OEPP103„317-322 Bull. OEPP 707\|vVarietal characteristics under french conditions of some lucerne cultivars selected for resistance to two pest insectslfHomoptera, Aphididae, Acyrthosiphon pisum, Fabaceae, Medicago sativa, RPI, RŽsistance, Lutte varietale Brabant, P. Le Boulc'h, V. 1993.(L'exploitation des ressources gŽnŽtiquesPhytomad 452  41-45dNi 0460lhbsŽlection, rŽsistance, plante, insecte, QTL, retrocroisement, sŽlection reccurente, RFLP, marqueur 0$²‚ÒR’4àúšò:XRBrown, S.M. Greenplate, J.T. Isaac, B.G. Jennings, M.G. Levine, E.B. Purcell, J.P. 1994 1-52,%Brevet- #PCT/US94/02306 - WO 94/21805æ 4738haBrevet, Patatine, Esterase, $TOXPROT, Toxicite, Lepidoptera, Solanum tuberosum, lectine, insecte,.'Method of controlling insects in plants^XBurgess, E.P.J. Main, C.A. Stevens, P.S. Christeller, J.T. Gatehouse, A.M.R. Laing, W.A. 1994J. Insect. Physiol.ò"Journal of Insect Physiology409<803-811nNi 0151üpjGrowth and survival responses were determined for the black field cricket Teleogryllus commodus fed 6 different protease inhibitors (SBTI, WGI-1, POT-1, POT-2, BPTI and CpTI), either singly or in combination, at a range of concentrations in diets containing 3 different levels of casein. Several inhibitors caused high levels of mortality at concentrations as low as 0.1% (w/v) on diets with low or moderate casein. In all cases the efficacy of the protease inhibitors in reducing cricket growth was strongly influenced by the level of dietary casein as well as by the concentration of the inhibitor. POT-2 and SBTI were particularly effective. Two-way combinations of protease inhibitors caused significant mortality and reduced growth as effectively as the best single inhibitors at all dietary casein levels. A synergistic effect was obtained from the combination of POT-1 (binds strongly to SAAPLpNA hydrolysing enzyme) and WGI-1 (binds strongly to trypsin). A time-series study using POT-2 showed that this inhibitor caused continual suppression in the activity of the digestive endopeptidases trypsin and SAAPLpNA hydrolysing enzyme, but no reduction in the activity of the exopeptidase leucine aminopeptidase. Increased levels of enzyme inhibition at the higher POT-2 concentration were directly reflected in the feeding trials where greater growth suppression was also observed.f_Article EPJ Burgess, Hort & Food Res Inst New Zealand, Private Bag 92169, Auckland, New ZealandVä Effects of protease inhibitor concentration and combinations on the survival, growth and gut enzyme activities of the black field cricket, Teleogryllus commodus ‹   f`protease inhibitors; Orthoptera; Teleogryllus commodus; insect rŽsistance; digestive protease activity; PLANT PROTEINASE-INHIBITORS; COWPEA VIGNA-UNGUICULATA; TRANSGENIC TOBACCO PLANTS; TRYPSIN-INHIBITORS; INSECT RƒSISTANCE; CALLOSOBRUCHUS-MACULATUS; BACILLUS-THURINGIENSIS; DIGESTIVE PHYSIOLOGY; MECHANISM; DEFENSE, mode d'action, inhibiteur protease, Caillaud, M. 1996ÈpCaractŽrisation de l'interaction Triticum/S. avenae et analyse des mŽcanismes de la rŽsistance des T. monococcum ! 3 b  $Marina Caillaud - INRA Rennesüavril 96Rapport d'activitŽNi 1197\VHomoptera, aphididae, rŽsistance, plante, insecte, puceron, sŽlection, mecanisme de la rŽsistance, EPG, RPI, physiologie, biochimie, analyse multivariŽe, ACP, AFC, antiappŽtent, phagostimulant, acide hydroxamique, DIMBOA, acide aminŽ, sve, phlome, callose, genetique, variabilite, durabilite, gestion de la rŽsistance, biotype, agressivitŽ,0)callahan, F.E. davis, F.M. Williams, W.P. 1992tnSteady-state polypeptide profiles of whorl tissue from lepidoptera-resistant and susceptible corn inbred lines Crop Science32 1203-1207Ni 1195 rŽsistance, insecte, mais, sŽlection, mecanisme, RPI, Zea mays, Spodoptera frugiperda, Diatraea grandiosella, test, biochimie, proteine, purification, milieu artificiel, electrophorese 2D, genotype, cysteine, immunomarquage, immunoblot, proteinase, sequencage, biomol,$Carlini, C.R. Guimaraes, J.A. 1991NHPlant and microbial toxic proteins as hemilectins: emphasis on CanatoxinToxicon29791-806 25684-Lectine, Toxine, Induction, $toxprot, insecte"Carrire, Y. Roitberg, B.D.R 1995"ÞEvolution of host-selection behaviour in insect herbivores: genetic variation and covariation in host acceptance within and between populations of Choristoneura rosaceana (Family: Tortricidae), the obliquebanded leadfoller “ ª Heredity74357-368Ni 0377 ²mEvolution, comportement, polymorphisme, genetique quantitative, Choristoneura rosaceana (Family: Tortricidae) @ W 2,Chen, J.Q. Delobel, B. RahbŽ, Y. Sauvion, N. 1996b[Biological and chemical characteristics of a genetic resistance of melon to the melon aphidpEntomol. exp. appl.› Printed in Belgium80250-253.'Entomologia Experimentalis et ApplicatadNi 1196pÿinteraction plante insecte, rŽsistance, puceron, plante, homoptera, aphididae, gene vat, biochimie, RPI, melon, cucumis melo, cucurbitacee, Aphis gossypii, pyrazole, amino acide, phloeme, electrophorese, EPG, comportement; milieu artificiel, test de choixhbIXth International Symposium on Insect-Plant Relationships - June 24/30, 1995, Gwatt (Switzerland)2,Chino, M. Fukumorita, T. Kawabe, S. Ando, Y. 1981xx x-x 2900¢œAminoacide, Phloeme, Saccharose, $PHLOEM, Stylectomie, Homoptera, Cicadellidae, Oryza sativa, Poaceae, pH, Potassium, Mineral, Pression osmotique, Laser YAGNGChemical composition of rice phloem sap collected by "insect" techniqueG$Chrispeels, M.J. Raikhel, N.V. 1991 Plant Cell3 1-9Ì 2565<6Lectins, lectin genes, and their role in plant defense:3Lectine, RŽsistance, Genetique, insecte, gŽnŽralitŽeCohen, E. Casida, J.E. 1990 Pestic. Biochem. Physiol.37249-253 2050œ•Insecta, Champignon, Chitine synthase, Lectine, Peptide, Acide nucleique, Inhibition, Activation, Biosynthese, N-acetylglucosamine, $TOXPROT, insecteº~xInsect and fungal chitin synthetase activity : specificity of lectins as enhancers and nucleoside peptides as inhibitors Cole, R.A. 1994î½Isolation of a chitin-binding lectin, with insecticidal activity in chemically-defined synthetic diets, from two wild Brassica species with resistance to cabbage aphid Brevicoryne brassicae ¨ 722d181-187 Ni 0144èâBrassica fruticulosa; Brassica spinescens; Brevicoryne brassicae; lectin; host-plant rŽsistance; chitin; artificial diets; chitinase; WHEAT-GERM-AGGLUTININ; GEL-ELECTROPHORESIS; ACYRTHOSIPHON-PISUM; PLANT; RICE, WGA;, lectine,LFArticle RA Cole, Hort Res Int, Wellesbourne CV35 9EF, Warwick, England.'Entomologia experimentalis et applicatadEntomol. exp. appl.eJDCouty, A. de la Vina, G. Clark, S.J. Pham-Delgue, M.-H. Poppy, G.M. 2001ô¯Direct and indirect sublethal effects of Galanthus nivalis agglutinin (GNA) on the development of the potato-aphid parasitoid, Aphelinus abdominalis (Hymenoptera: Aphelinidae)u  ” "Journal of Insect Physiology47553-561 "Journal of Insect PhysiologyNin>lectines, GNA, mode d'action, Hemiptera, Aphelinus abdominalis )  JIP°XQCouty, A. Down, R.E. Gatehouse, A.M.R. Kaiser, L. Pham-Delgue, M.-H. Poppy, G.M.ü 2001ä Effects of artificial diet containing GNA and GNA-expressing potatoes on the development of the aphid parasitoid Aphidius ervi Haliday (Hymenoptera: Aphidiidae) q ~ "Journal of Insect Physiology47 1357-1366 "Journal of Insect PhysiologyNiz6lectines, GNA, mode d'action, Hemiptera, Aphidius ervi ) 6  JIP@&Z%*$D# !B ²"@X! WËð–x8Í_ –x”`K–xË,& 0! "ÀXWË°"H?ƒÞx }!  Cronshaw, J. Sabnis, D.D. 1989Phloem proteins "BEHNKE, H.D., SJOLUND, R.D.HASieve elements - comparative structure, induction and developmenti Berlin Springer257-283d 2218zsPhloeme, Proteine PP, Revue, MET, Lectine, Ultrastructure, $PHLOEM, $toxprot, insecte, Cucumis melo, Cucurbitacees,¤Czapla, T.H. Lang, B.A. 1990šEffect of plant lectins on the larval development of European Corn Borer (Lepidoptera : Pyralidae) and Southern Corn Rootworm (Coleoptera : Chrysomelidae) X a Œ ™ J. econ. Entomol.›83 2480-2485$Journal of Economic Entomology 2264²¬Coleoptera, Chrysomelidae, Lectine, $TOXPROT, Developpement larvaire, Lepidoptera, Pyralidae, Ostrinia nubilalis, RPI, RŽsistance, Toxicite, mode d'action, insecte, binding Czapla, T.H. 1994 1-28,&Brevet - #PCT/US94/00630 - WO 94/16565 4735ŽˆAprotinine, Inhibiteur protease, Brevet, $TOXPROT, Synergie, Lectine, WGA, Ostrinia nubilalis, Lepidoptera, Bowman-Birk, insecte, brevetÆ¿Aprotinin and synegistic combinations thereof with lectins as larvicides against insect pests of agronomic crops, harvested material thereof, and products obtained from the harvested materialt Czapla, T.H. 1997D=Plant lectins as insect control proteins in transgenic plants Carozzi, N., Koziel, M.p@9Advances in insect control: the role of transgenic plantsp  London (GBR) Taylor & Francis123-138d6663, Ni>8Lectine, Revue, Transgenose, Resistance, Lutte varietaleNGDawson, G.W. Griffiths, D.C. Pickett, J.A. Wadhams, L.J. Woodcock, C.M.p 1987xrPlant-derived synergists of alarm pheromone from turnip aphid, Lipaphis (Hyadaphis) erysimi (Homoptera, Aphididae)J. chem. Ecol.J. chem. Ecol.137 1663-1671ÿüöInsecta, Arthropoda, Invertebrata, Homoptera, Pheromone alarme, Activite biologique, Synergie, Isothiocyanate organique, Origine vegetale, Electrophysiologie, Sesquiterpene, Hydrocarbure, Depredateur, RPI, Aphididae, Lipaphis erysimi, B-Farnesene 1523b[de Jager, C.M. But™t, R.P.T. Klinkhamer, P.G.L. de Jong, T.J. Wolff, K. van der Meijden, E.  1995€OGenetic variation in Chrysanthemum for resistance to Frankliniella occidentalis  5 77277-287lNi 01045Þ×Dendrathema grandiflora, Frankliniella occidentalis, Thysanoptera, Thripidae, Oviposition preference, feeding damage, mode d'action, mŽcanisme rŽsistance, RPI, test de choix, screening, sŽlection variŽtale, insecte,  $Lydia.'Entomologia experimentalis et applicataaEntomol. exp. appl.ede Ponti, O.M.B. 1982TMPlant resistance to insects : a challenge to plant breeders and entomologistsÇ0)Vth Int. Symp. Insect-Plant Relationships  Wageningen337-347ïNi 0415nXQlutte intŽgrŽe, insectes, rŽsistance, sŽlection, gestion rŽsistance, variabilite,d"Dhillon, N.P.S. Wehner, T.C. 1991Trop. Pest Man.374421-428.Tropical Pest Management 3495`ZHost-plant resistance to insects in cucurbits: germplasm ressources, genetics and breedingpjrŽsistance, cucurbitaceae, insectes, Cucumis, genetique, sŽlection, revue, puceron, melon, lutte intŽgrŽe, +<üöInsecta, Arthropoda, Invertebrata, Homoptera, Pheromone alarme, Activite biologique, Synergie, Isothiocyanate organique, Origine vegetale, Electrophysiologie, Sesquiterpene, Hydrocarbure, Depredateur, RPI, Aphididae, Lipaphis erysimi, B-FarneseneWÌP˜•Insecta, Champignon, Chitine synthase, Lectine, Peptide, Acide nucleique, Inhibition, Activation, Biosynthese, N-acetylglucosamine, $TOXPROT, insecteˆƒInsecta, Helicoverpa zea, zea mays, resitance inheritance, Additive-dominance model, rŽsistance, plante, sŽlection variŽtale, mais, ¸ˆ…Insecta, Immunite, Revue, Developpement, Defense, Lectine, Reconnaissance cellulaire, Galactose, Expression stade specifique, insecte insectelt84insecte, comportement, revue, puceron, test de choix0Insecte, ImmunitŽINSECTe, intestin,s üinsecte, puceron, lectine, plante transgenique, homoptera, aphididae, test toxicite, microscopie, milieu artificiel, comportement, proteine, Nilaparvata lugens, nephotettix cinciteps, Galanthus nivalis, GNA, WGA, ConA, lipoxygenase, immunomarquage, METBInsecte, RŽsistance}d_insecte, rŽsistance, cotton genie genetique, transgenose, Chitinas, lectine, Bt, revue, insecteª°dainsectes, transgenese, inhibiteur de proteases, coleopteres, lectines, revue, plante transgŽniqueINSECTICIDAL ACTIVITY insecticidal crystal protein INSECTICIDEDOInsecticide RŽsistance! pmInsecticide, Lutte biologique, Virus, $TOXPROT, Neurotoxicite, Scorpionidae, Toxine, Baculovirus, LepidopteraÀ¼INSECTICIDES, lutte intŽgrŽe, plante resistante, insecte, IPM , Integrated Pest Management, gestion rŽsistance, Nephotettix virescens, Nilaparvata lugens, riz, lutte biologique, sŽlection,p insectsumINSECTS, Myzus persicaeSIHEINSECTS, Nicotiana tabacum, Medicago sativa, Solanum nigrum, $toxprot integrated pest managementàÝinteraction plante insecte, rŽsistance, puceron, plante, homoptera, aphididae, gene vat, biochimie, RPI, melon, cucumis melo, cucurbitacee, Aphis gossypii, pyrazole, amino acide, phloeme, electrophorese, EPG, comportement interactions tritrophiquesllaintestin, insecte, ME INVITROCE.Æ-R,Ž*Æ+ )Ð(Î'"2,Dogimont, C. Bordat, D. Pitrat, M. Pages, C. 1994Ì_Mise en Žvidence d'une rŽsistance ˆ Liriomyza trifolii (Burgess) chez le melon (Cucumis melo L) $ 6 P ^  Yv 4689, GŽ 1319, Ni 1118ø‹rŽsistance,Liriomyza trifolii (Burgess), melon (Cucumis melo L.), diptere, tomate, sŽlection, mecanisme rŽsistance, insecte, cucurbitacees,    0 ? Dorschner, K.W. 1993681 31-41 3918¼¶Aphids, like most phloem-feeding insects, commonly exhibit a high degree of host specificity. Plant-specific chemical compounds are likely to serve as important host selection cues for monophagous aphids and such substances could be present in aphid honeydew. Apterous virginoparae of Myzus persicae (Sulzer) and Phorodon humuli (Schrank) were reared on a buffered sucrose solution containing various aphid honeydews or a mixture of amino acids. In two separate experiments, the host-specific P. humuli (hop aphid) could grow and reproduce only on diets containing honeydew collected from hop (Humulus lupulus L.). M. persicae (the green peach aphid, GPA) did not perform well on diets containing hop honeydew, perhaps because hop is a poor GPA host. Honeydew collected from preferred GPA host plants rape, Brassica napus L., and jimsonweed, Datura stramonium L., allowed GPA growth and reproduction. Hop aphids, however, performed poorly on rape and jimsonweed honeydew diets. Bell pepper, Capsicum annuum L., honeydew supported neither the hop aphid nor GPA. The study of aphid honeydew components may contribute towards a more complete understanding of host preference and selection phenomena in aphids.nhArticle KW Dorschner, Univ Idaho, Dept Plant Soil & Entomol Sci, PARMA Res & Extens Ctr, PARMA, ID 83660xrSurvival, growth, and reproduction of two aphid species on sucrose solutions containing host or non-host honeydewsœ–miellat;milieu artificiel; Phorodon humuli; Myzus persicae; Monophagie; Polyphagie; Amino Acids; PERSICAE SULZER; HOMOPTERA; HOP, rŽsistance, puceron.'Entomologia experimentalis et applicatanEntomol. exp. appl.eDorschner, K.W. 1993zsSurvival, growth, and reproduction of two aphid species on sucrose solutions containing host or non-host honeydews.681 31-41 3918¼¶Aphids, like most phloem-feeding insects, commonly exhibit a high degree of host specificity. Plant-specific chemical compounds are likely to serve as important host selection cues for monophagous aphids and such substances could be present in aphid honeydew. Apterous virginoparae of Myzus persicae (Sulzer) and Phorodon humuli (Schrank) were reared on a buffered sucrose solution containing various aphid honeydews or a mixture of amino acids. In two separate experiments, the host-specific P. humuli (hop aphid) could grow and reproduce only on diets containing honeydew collected from hop (Humulus lupulus L.). M. persicae (the green peach aphid, GPA) did not perform well on diets containing hop honeydew, perhaps because hop is a poor GPA host. Honeydew collected from preferred GPA host plants rape, Brassica napus L., and jimsonweed, Datura stramonium L., allowed GPA growth and reproduction. Hop aphids, however, performed poorly on rape and jimsonweed honeydew diets. Bell pepper, Capsicum annuum L., honeydew supported neither the hop aphid nor GPA. The study of aphid honeydew components may contribute towards a more complete understanding of host preference and selection phenomena in aphids.nhArticle KW Dorschner, Univ Idaho, Dept Plant Soil & Entomol Sci, PARMA Res & Extens Ctr, PARMA, ID 83660œ–miellat;milieu artificiel; Phorodon humuli; Myzus persicae; Monophagie; Polyphagie; Amino Acids; PERSICAE SULZER; HOMOPTERA; HOP, rŽsistance, puceron.'Entomologia experimentalis et applicatanEntomol. exp. appl.eD=Down, R.E. Gatehouse, A.M.R. Hamilton, W.D.O. Gatehouse, J.A. 1996:ÎSnowdrop lectin inhibits development and decreases fecundity of the glasshouse potato aphid (Aulacorthum solani) when administered in vitro and via transgenic plants both in laboratory and glasshouse trials ] o ƒ ‹ J. Insect Physiol.42 11-12 1035-1045d"Journal of Insect Physiology 6095, Nicx° JIP›jcDown, R.E. Ford, L. Woodhouse, S.D. Raemaekers, R.J.M. Leitch, B. Gatehouse, J.A. Gatehouse, A.M.R." 2000À|Snowdrop lectin (GNA) has no acute toxic effects on a beneficial insect predator, the 2-spot ladybird (Adalia bipunctata L.) g x "Journal of Insect Physiology46379-391€"Journal of Insect Physiology Nic"lectine, mode d'action, GNA JIPDrif, L. Brehelin, M. 1989J. Insect Physiol.3510729-736¸ 1815tmOrthoptera, Locusta migratoria, Agglutinine, Lectine, Immunite, Hemolymphe, Hemocyte, Reconnaissance, insecte ²FAgglutinin mediated immune recognition in Locusta migratoria (Insecta) * < > E Drif, L. Brehelin, M. 1994$Insect. Biochem. Molec. Biol.0)Insect Biochemistry and Molecular Biology243T283-289üNi 0031Ž‡Insecte, ImmunitŽ; Agglutinin; Lectine; Isoelectrofocusing; Affinity Chromatographie d'affinitŽ; recepteur, binding, Locusta migratorianpjArticle M Brehelin, Inra, Pathol Comparee Lab, CNRS, Ura 1184, Pl E Bataillou, F-34095 Montpellier, France¬hPurification and characterization of an agglutinin from the hemolymph of Locusta migratoria (Orthoptera) I [  Edmonds, H.S.ÿ 1994 UniversitŽ de Durham (GB) phD Thesis 4350¾yAntimetabolic proteins from plants and their potential use in conferring resistance against corn rootworms, Diabrotica spn l y ®iAntimetabolic proteins, plante, rŽsistance, corn rootworms, Diabrotica sp., $toxprot, lectine, insecte,n > K 2þ120&/ l Ehler, L.E.d 1995jdBiological control of obscure scale (Homoptera: diaspididae) in California: an experimental approachEnviron. Entomol. *#9301 Annapolis Rd, Lanham, MD 20706n Entomol Soc Amer244o779-795Environmental Entomology 0046-225XPNi 0577º´Melanaspis obscura; Encarsia aurantii; $lutbio, aphididae, homoptera; MALACOSOMA DISSTRIA , LEPIDOPTERA; FOREST TENT CATERPILLAR; APHELINIDAE HYMENOPTERA; LASIOCAMPIDAE; PARASITISM , %Obscure scale, Melanaspis obscura (Comstock), is native to the eastern half of the United States where it is associated with hosts in the genera Quercus, Carya, and Castanea. In its native home, the scale is exploited by a complex of natural enemies, including predators, parasites, and pathogens. Although obscure scale is generally maintained at low levels in natural habitats (presumably by natural enemies), it is a major pest of pin oak in urban areas and a minor pest of pecan. In 1962, an infestation of obscure scale was detected on oaks in Capitol Park in Sacramento, CA; efforts to eradicate the infestation were not successful, and this population became a target for classical biological control in 1981: Because the infestation was restricted and spread slowly, there was sufficient time for preintroductory investigations. Exploration for candidate natural enemies for importation into California was directed at parasites associated with obscure scale on pecan in southern Texas. Eleven species in 8 genera were recovered; the major species were Ablerus clisiocampae (Ashmead), Coccophagoides fuscipennis (Girault), Encarsia aurantii (Howard), and Physcus varicornis (Howard). Instead of releasing all of the major primary parasites (empirical approach), a more experimental approach was employed-that is, single species release of E. aurantii. This species was chosen because of its thelyotokous reproduction, high egg load at emergence (highest among major primary parasites), and abundance in the native home of obscure scale. Over 11,000 females were released in 1988 and establishment was confirmed in 1990. From 1992-1994, the parasite population increased steadily while the abundance of scale crawlers declined by 3-fold; the crawler-to-parasite ratio declined from approximate to 25 to approximate to 7. Through selective pruning, parasitization by E. aurantii, and timing of insecticide treatments, obscure scale is now under integrated pest management (IPM) in Capitol Park, and it may eventually come under complete biological control. This project illustrates how preintroductory investigations both in the native home of the target pest and under quarantine conditions can be used to derive an introduction strategy in classical biological control. Some additional aspects of introduction strategy are discussed.ELEArticle LE Ehler, Univ Calif Davis, Dept Entomol, Davis, CA 95616 USAž$Eigenbrode, S.D. Trumble, J.T. 1994J. Agr. Entomol.("Journal of Agricultural Entomology113201-224Ni 0189¤žHost plant resistance to insects (PRI) is an underutilized pest management strategy in vegetable production. Increased pressures to reduce pesticides, and changes in technology now increase the economic viability and probable role of PRI in vegetable pest management. This is reflected in the relatively recent release of several insect-resistant varieties and breeding lines. The attention PRI now receives in extension publications is also increasing. There is room to improve research and extension documentation to assist producers in making better use of the available resistance to insects in vegetable crops. In the short term, existing varieties can be screened more extensively and quantitative information provided to producers. In the long term, variety specific recommendations for the use of chemical controls, and other management tactics in conjunction with PRI will be beneficial. Awareness of varietal susceptibility to insect pests will increase the incentives to private breeders to eliminate extremely susceptible material from their breeding programs. Trends in these directions can already be seen in the industry. Support for the research necessary to exploit PRI in vegetables will be required from public sources, as part of the alternatives to pesticides, and from private breeders and producers who stand to benefit from the development of variety-specific recommendations and impartial comparison of varieties.^WReview SD Eigenbrode, Univ Arizona, Dept Entomol, 410 Forbes Bldg, Tucson, AZ 85719 USAòXQHost plant resistance to insects in integrated pest management in vegetable cropsò2+vegetables; host plant rŽsistance; integrated pest management; ONION THRIPS THYSANOPTERA; ECONOMIC INJURY LEVELS; SORGHUM MIDGE DIPTERA; SWEET-POTATO; BACILLUS-THURINGIENSIS; BRASSICA-OLERACEA; SPODOPTERA-EXIGUA; BREEDING LINES; SAMPLING PLANS; CULTIVARS, lutte intŽgrŽe, insecte, rŽsistance, planteòZSEisemann, C.H. Donaldson, R.A. Pearson, R.D. Cadogan, L.C. Vuocolo, T. Tellam, R.L. 1994ŠFLarvicidal activity of lectins on Lucilia cuprina: mechanism of action " 1 Entomol. exp. appl.›72 1-10.'Entomologia Experimentalis et Applicata›Ni 0114ˆDlectine, Lucilia cuprina:, mode d'action, $toxprot,insecte, FITC, ME    RKDr C.H. Eisemann CSIRO Division of Tropical Animal Production Australia JIPŒ<6Erb, W.A. Lindquist, R.K. Flickinger, N.J. Casey, M.L. 1994®iResistance of selected interspecific Lycopersicon hybrids to greenhouse whitefly (Homoptera: Aleurodidae)ý % 1  Fla. Entomol.771104-116þFlorida EntomologistdemendŽ le 10/11/94^@9insecta; Trialeurodes vaporariorum spp; tomato, aleurodesêLycopersicon interspecific hybrids and species inbreds were examined for resistance to the greenhouse whitefly, Trialeurodes vaporariorum (Westwood) (Homoptera: Aleurodidae), in four separate greenhouse studies. The two L. pennellii Correll interspecific hybrids (ICR.13 X LA1735 and ICR.13 X LA716) were the most toxic and/or repellent to adult whiteflies. ICR.13 X LA1735 exhibited the most adult and nymphal antibiosis and adult antixenosis, supported the lowest number of eggs and nymphs and developed the smallest second generation of adults. The L. esculentum Miller entry (ICR.13) was usually intermediate in all characteristics examined. All the entries in the study were able to support all the whitefly developmental stages which suggests selective pressure could possibly overcome a resistance mechanism based solely on adult antibiosis. This study provides evidence for adult and nymphal antibiosis mediated by trichome exudates and the possibility that a second nymphal antibiosis mechanism is present within the leaves of LA1735.VHAArticle WA Erb, Ohio State Univ, Dept Hort, Wooster, OH 44691 USA¼ >¸=„<9(;ê:,8ª7x6ä5„43HJDEscriche, B. Martinez-Ramirez, A.C. Real, M.D. Silva, F.J. FerrŽ, J. 1994&Arch. Insect. Biochem. Physiol. 4.Archives of Insect Biochemistry and Physiology264*315-327ÚNi 0120ztBacillus thuringiensis; Phthorimaea operculella; insecticidal crystal protein; recepteur, mode d'action, binding; BtvpThe potato tuber moth is susceptible to at least three insecticidal crystal proteins (ICPs) from Bacillus thuringiensis: CrylA(b), CrylB, and CrylC. To design useful combinations of toxin genes either in transgenic plants or in new genetically modified B. thuringiensis strains, it is necessary to determine the binding characteristics of the different ICPs so as not to combine a pair sharing the same binding site. This has been accomplished using two different techniques: I-125-labeling of the ICPs with further measurement of the radioactivity bound to brush border membrane vesicles, and microscopic visualization of the bound ICPs by enzyme-linked reagents such as antibodies or streptavidin using biotinylated ICPs. Our results st-cow that CrylA(b), CrylB, and CrylC bind to different sites in the brush border membrane of midgut epithelial cells. Also, the affinity of the binding sites for the ICPs and their concentration in brush border membrane vesicles has been determined in a laboratory strain and a storage collected population. No significant differences were found between these two strains. (C) 1994 Wiley-iiss, Inc.ZTArticle B Escriche, Univ Valencia, Fac CC Biol, Dept Genet, E-46100 Burjassot, Spain"¶Occurrence of three different binding sites for Bacillus thuringiensis delta-endotoxins in the midgut brush border membrane of the potato tuber moth, Phthorimaea operculella (Zeller) 0 F – ­ Estada, U. Ferre, J. 1994 Appl. Environ. Microbiol.­6010 3840-3846 ,&Applied and Environmental MicrobiologyNi 0316 ÊÄDIAMONDBACK MOTH LEPIDOPTERA; POTATO BEETLE COLEOPTERA; DELTA-ENDOTOXIN; HELIOTHIS-VIRESCENS; TRICHOPLUSIA-NI; TOBACCO BUDWORM; SUBSP KURSTAKI; MEMBRANE; SPECIFICITY; recepteur, Bt, modee d'actionVPArticle J Ferre, Univ Valencia, Fac CC Biol, Dept Genet, E-46100 Valencia, SpainPãBinding of insecticidal crystal proteins of Bacillus thuringiensis to the midgut brush border of the cabbage looper, Trichaplusia ni (Hubner) (Lepidoptera: Noctuidae), and selection for resistance to one of the crystal proteinst , B u „  Etzler, M.E. 19860*Distribution and function of plant lectinsRKThe lectins: properties, functions and applications in biology and medecinen  Orlando (USA)A HBLiener, I.E. ; Sharon, N. ; Goldstein, I.J. , Acadamic Press, Inc.371-437 biblio labo hb$toxprot, lectine, Con A, GNA, mode d'action, revue, biologie molŽculaire, reconnaissance, insectejdFabre, C. Causse, H. Mourey, L. Koninkx, J. Riviere, M. Hendriks, H. Puzo, G. Samama, J.P. Rouge, P. 1998æ¡Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv. RAZ-2) seedsn {   Biochem. J.¢ 329¼551-560 Biochem. J.üLFArcelin, Lectine, Phaseolus vulgaris, Graine, Binding, OligosaccharideXRFaye, L. Fitchette-Laine, A.C. Gomord, V. Chekkafi, A. Delaunay, A.M. Driouich, A. 1993 6/N.H. Battey, H.G. Dickinson & A.M. Hetherington2+Post-translationnal modifications in plants  Cambridge 213-242T82Society for Experimental Biology Seminar Series 53 3599ìåN-linked glycan, high-mannose type oligosaccharide, Con A, glycoproteine, lectine, affinodetection, immunodetection, biosynthese, maturation, fonction, interaction cellulaire, revue, $toxprot, plante, insecte, lectine, gŽnŽralitŽô`YDetection, biosynthesis and some functions of glycans N-linked to plant secreted proteinsô*#Ferrari, C. Barbieri, L. Stirpe, F.P 1991‚QEffects of plant ribosome-inactivating proteins on ribosomes from Musca domestica B Comp. Biochem. Physiol. 100B2223-227 3018ª£Ribosome, Toxine, $TOXPROT, Lectine, Proteine RIP, Musca domestica, Toxicite, Diptera, Phenylalanine, Traduction, Glycosidase, Saporine, Ricine, Eucaryote, insecte˜4-Fitches, E. Gatehouse, A.M.R. Gatehouse, J.A. 1997ú¶Effects of snowdrop lectin (GNA) delivered via artificial diet and transgenic plants on the development of tomato moth (Lacanobia oleracea) larvae in laboratory and glasshouse trials x Š J. Insect Physiol.438727-7390"Journal of Insect Physiology Nic†€Lectine, Galanthus nivalis, Amaryllidaceae, Lepidoptera, Transgenose, Lacanobia oleracea, Solanaceae, Resistance, $TOXPROT, $TRG JIP‘"Fitches, E. Gatehouse, J.A.d 1998è¤A comparison of the short and long term effects of insecticidal lectins on the activities of soluble brush border enzymes of tomato moth larvae (Lacanobia oleracea) ‘ £ "Journal of Insect Physiology44 1213-1224"Journal of Insect Physiology Nicd3mode d'action, lectine, insecte, Lacanobia oleracea !  JIP Fitches, E.à 1999~xThe mechanisms of action of insecticidal lectins from snowdrop (GNA) and jackbean (Concanavalin A) on tomato moth larvaeUniversity of Durham Durham University of Durham PhD thesis ˆ demander"GNA, mode d'action, insecte, JIPf`Fitches, E. Ilett, C. Gatehouse, A.M.R. Gatehouse, L.N. Greene, R. Edwards, J.P. Gatehouse, J.A. 2001¾The effects of Phaseolus vulgaris erythro- and leucoagglutinating isolectins (PHA-E and PHA-L) delivered via artificial diet and transgenic plants ont he growth and development of tomato moth (Lacanobia oleracea) larvae; lectin binding to gut glycoproteins in vitro and in vivo  ! Â Ô     "Journal of Insect Physiology47 1389-1398"Journal of Insect Physiology Nicdd3mode d'action, lectine, insecte, Lacanobia oleracea0 !  JIP0@9Fitches, E. Woodhouse, S.D. Edwards, J.P. Gatehouse, J.A. 2001fÑIn vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; ConA) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal actionà * ; [ o ” ¦ "Journal of Insect Physiology47777-787"Journal of Insect Physiology Nicdd3mode d'action, lectine, insecte, Lacanobia oleraceaÐ !  JIP0LFFoissac, X. Thi Loc, N. Christou, P. Gatehouse, A.M.R. Gatehouse, J.A. 2000H³Resistance to green leafhopper (Nephotettix virescens) and brown planthopper (Nilaparvata lugens) in transgenic rice expressing snowdrop lectin (Galanthus nivalis agglutinin; GNA)   5 N ` ‘ ¢ "Journal of Insect Physiology46573-583"Journal of Insect PhysiologyNi¬glectines, GNA, mode d'action, Hemiptera, Nephotettix virescens, Nilaparvata lugens, plante transgenique ) S  JIP @@ ÏÂgpec•n‡Ž%EF}€5D^hqwxy{´µ#G¼“,N„É "LS[‰‹œ¢&8KP_`ablm|‚š¯ÈË@JXfŠ£ÊÌ ()7BCQU\ist‘’—˜›¦©«¶¹Í  '-.01234AOY]oruv~…†ŒžŸ¥§¨¬°±³º½Å$/?HMRWdjƒ”–¤ª®¸»¾¿ÀÁÃÆÇ+­²Ä!:zˆ6;ITZk™ ¡9·*>V<=ÎÏ. Adventitious shoot buds were induced 4 weeks after infection. Shoots were excised, elongated, and rooted on selection medium containing kanamycin. Needles from greenhouse-grown plants were confi„€ÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿÿîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîîon, 17-21/09/1997¢ Bruxelles (Bel)d CCE¢ 1-16tmLectine, Revue, Transgenose, Lutte varietale, Bacillus thuringiensis, Insecta, RPI, Mannose, ***SciSynPerssCLÐ RahbŽ, Y.  1998.(Engineering plants for insect resistance van Damme, E., Peumans, W.~xPerspectives of Plant lectin applications in Nutrition, Biotechnolgy and Therapy, COST 98 meeting, Genk (Bel), 4-7/04/98 Bruxelles (Bel)¡ CCE› 1-1 >8Lectine, Bacillus thuringiensis, Revue, ***SciArtPriComm $ÈPPERITROPHIC MEMBRANEPERSICAE SULZERelpHcroPHAoaPhaseolus limensis! Phaseolus vulgaris! PHASEOLUS VULGARIS L”Phaseolus vulgaris, Acanthoscelides obtectus, Callosobruchus maculatus, mode d'action , lectine, intestin, $toxprot, toxicite, tolerance,insecte&PHASEOLUS-VULGARISENCphloem specificnt,'Phloem, EDTA, stylectomie, CAM plantes,”`xrPhloeme, Homoptera, Aphididae, Stylectomie, Proteine PP, Lectine, Exsudation, Aminoacide, Sterol, $PHLOEM, insecte 0xsPhloeme, Proteine PP, Revue, MET, Lectine, Ultrastructure, $PHLOEM, $toxprot, insecte, Cucumis melo, Cucurbitacees, 0Phorodon humulielPhthorimaea operculella  Phyllocolpa Phyllonorycter salicifoliellaphylogeny, 18S rDNA physiological interactions–xPHYTOPHAGOUS INSECTS( Pirimicarb Pr Pisum sativumPLANAR LIPID BILAYERSPLANT Plant Defense PLANT PROTEINASE-INHIBITORS–xPlant Recognitionplant volatilesgr PLANT-LECTINS PLANT-VIRUSESplante rŽsistanceHDplante transgŽnique, Bt, rŽsistance, plante, insecte, TRANSFORMATION ýplante, rŽsistance, lectine, insecte, $toxprot, homoptere,revue, lepidoptere, coleoptere, WGA, Empoasca fabae, PHA, ConA, Acyrthosiphon pisum, GNA, Galanthus, Concanavaline, Lucilia cuprina, mode d'action, Heliothis virescens, Callosobruchus maculatus, PLANTSENEplasma membrane PLASMA-MEMBRANETP POKEWEED ANTIVIRAL PROTEIN PolyphagieicaPOPULATIONS, $lutchimpotassium pumpe  potato beetlePOTATO BEETLE COLEOPTERATPOTATO LEAFHOPPERýPOTATO,( E)-2-hexenal, (E)-2-heptenal, 1-octenol-3, hexyl acetate, (Z)-3-hexenyl acetate, hexanol-1,hexanal, 2-heptanone, 3-octanone, 4-methoxybenzaldehyde (p-anisaldehyde), hexanonitrile, heptanonitrile, 1,6-hexanedithiol, butyl isothiocyanate, 4-pent PREDATIONPROBING BEHAVIORNProgrammed Cell DeathPROGRAMMED CELL-DEATHprotease inhibitors PROTEINATProtein Synthesis Proteinase Inhibitor Genes,)proteine PR, Wheat Germ Agglutinin (WGA) PROTEINSE PROTEINS, recepteur, Bt, BBMN PROTON PUMPRA PROTOPLASTSSS PSYCHODIDAETT¤ puceron, Aulacorthum solani, lectine, mode d'action, GNA, Galanthus nivalis, Nilaparvata lugens, croissance , fecondite, transgenose, poster, Lacanobia oleracea° PURIFICATIONs QUISQUALATEbi0+recepteur, binding, insecte, SOLUBILIZATION ,&recepteur, binding, Locusta migratoria recepteur, Bt, modee d'action$!recepteur, mode d'action, bindingredox REGENERATIONS repellentstilREPRODUCTION, revueS(¤ resistance, plante, Homoptera, Aphididae, comportement, electroantennographie, EAG, allŽlochimique, RPI, Sitobion avenae (F.), Metopolophium dirhodum (Walk.),À RESISTANT,(RESOLUTION 2-DIMENSIONAL ELECTROPHORESIS` RESPONSESàÛRevue, $ARYL, Insecta, Proteine LSP, Hemolymphe, Stockage, Lipophorine, Lipide, Transport, Vitellogenine, Immunite, Lectine, Inhibiteur protease, Phenoloxydase, Peptide, Coagulation, Chromoproteine, Arylphorine, insecte€}Revue, Coleoptera, Lepidoptera, Homoptera, Proteine, Inhibiteur enzyme, Inhibiteur protease, Lectine, Resistance, TransgenosetoRevue, Genie genetique, RPI, RŽsistance, Lectine, Inhibiteur protease, Bacillus thuringiensis, Toxine, $TOXPROT |xRevue, RŽsistance, Insecte, Transgenose, Lutte varietale, Inhibiteur protease, $TOXPROT, Bacillus thuringiensis, lectinelhrevue, rŽsistance, proteine, inhibiteur protease, lectine, transgenose, proteine PR, reponse HP, insecteÀ‹Revue, Transgenose, Resistance, Proteine, Inhibiteur enzyme, Inhibiteur protease, Lectine, Bacillus thuringiensis, Transformation genetiqueÀXÌÇRevue, Transgenose, RŽsistance, Proteine, Inhibiteur protease, Bacillus thuringiensis, Vigna unguiculata, Lutte varietale, Genie genetique, $TOXPROT, lectine, gŽnŽralitŽ, insecte, inhibiteur proteaseÌ CB–AF?@,ecte, $toxprot, homoptere,revue, lepidoptere, coleoptere, WGA, Empoasca fabae, PHA, ConA, Acyrthosiphon pisum, GNA, Galanthus, Concanavaline, Lucilia cuprina, mode d'acFritz, R.S. Sims, E.L. 1992TNPlant resistance to herbivores and pathogens. Ecology, Evolution, and Genetics Chicago &The University of Chicago PressHNi 01100bouquin perso a YvanTNrŽsistance, plante, insecte, ecologie, revue, evolution, genetique, sŽlection, Fritz, R.S. 1995LFDirect and indirect effects of plant genetic variation on enemy impactEcol. Entomol. 0*Osney Mead, Oxford, United Kingdom OX2 0EL Blackwell Science Ltdÿ201 18-26Ecological Entomology  0307-6946 Ni 0416TJDArticle RS Fritz, Vassar Coll, Dept Biol, Poughkeepsie, NY 12601 USA²«Phyllocolpa; Phyllonorycter salicifoliella; Salix sericea; interactions tritrophiques ; rŽsistance plante, gestion rŽsistance, variabilite, insecte, sŽlection, variabiliteA,%Fry, K.L. Seaton, D.S. Sandeman, R.M. 1994Int. J. Parasitol.243o379-387o,&International Journal for ParasitologyNi 0325 ª£Monoclonal Antibodies; Lucilia cuprina; Sheep Blowfly; Midgut Antigens; electrophorese 2D; Immunohistologie; immunite, anticorps monoclonaux; intestin, insecte, ME PJArticle RM Sandeman, La Trobe Univ, Sch Agr, Bundoora, Vic 3083, Australia¤_The production and characterisation of monoclonal antibodies to Lucilia cuprina larval antigensS @ O .'Fuchs, R.L. Berberich, S.A. Serdy, F.S. 1993 *#John A. Thomas and Laurie A. Myers.*#Biotechnology and safety Assessmentg New York Raven Press, Ltd..199-212 4314d^Safety evaluation of genetically engineered plants and plant products: insect-resistant cottonf_insecte, rŽsistance, cotton genie genetique, transgenose, Chitinas, lectine, Bt, revue, insectenFurk, C. Hines, C.M. 1993ªfAspects of insecticide resistance in the melon and cotton aphid, Aphis gossypii (Hemiptera, aphididae) A O Ann. Appl. Biol. 123a1 9-17 Annals of Applied Biology  4451ÈÁAphis-Gossypii; Insecticide RŽsistance; Cucumber; Chrysanthemum; Electrophoresis; Host Plant Preference; Pirimicarb; Diazinon; Heptenophos; FIELD POPULATIONS; GLOVER, puceron, aphid, IsoenzymesrĽStrains of the aphid Aphis gossypii, taken from cucumber in UK glasshouses were tested for resistance to pirimicarb, diazinon and heptenophos. Compared to a susceptible strain, resistance factors th diazinon of up to 659 were found in populations collected between 1987 and 1989. Compared to the same susceptible strain, diazinon-resistant populations also showed a reduced response to heptenophos. All field populations tested against pirimicarb were resistant. Host plant preference tests showed that all strains (including stock cultures) tested could readily breed on cotton. However strains originally collected from chrysanthemum did not transfer to cucumber and likewise strains from cucumber would not colonise chrysanthemum. Polyacrylamide gel electrophoresis of four of the aphid strains showed differences in migration rates and intensity of staining of esterase bands. Intensity of staining was correlated with the degree of diazinon resistance.c\VArticle C Furk, Maff, Pesticides Safety Directorate, Harpenden AL5 2SS, Herts, EnglandKLìN¬GÄDF‚E6; Empoasca fabae; PHA; WGA; Phaseolus vulgaris; Phaseolus limensis; Lens culinaris; Pisum sativum; Arachis hypogaea; Dolichos bifloris; Glycine max, Griffonia simplicifolia, Bauhinia purpurea, Triticum vulgaris (WGA), Artocarpus integrifolia, Codium fragile, Amaranthus caudatus, lectine, insecte¦l›”›– -v P-† lectinWËp-v ! WËð–x8Í_ –x”`K–xË(o 0&! "ÀXWË°$Gatehouse, A.M.R. Boulter, D. 1983J. Sci. Food Agric.ºJ. Sci. Food Agric.34345-350– 36594D©Assessment of antimetabolic effects of trypsin inhibitors from Cowpea (Vigna unguiculata) and other legumes on development of the bruchid beetle Callosobruchus maculatusn G X ‘ ¨¢Coleoptera, $TOXPROT, Inhibiteur protease, Trypsine, Fabaceae, RPI, RŽsistance, Vigna unguiculata, Bruchidae, Callosobruchus maculatus, Toxicite, lectine, insecteF?Gatehouse, A.M.R. Dewey, F.M. Dove, J. Fenton, K.A. Pusztai, A.ˆ 1984ðƒEffect of seed lectins from Phaseolus vulgaris on the development of the larvae of Callosobruchus maculatus: mechanism of toxicity"  / T l J. Sci. Food Agric. 35373-380ƒ4.The Journal of Science of Food and Agriculture 3620¼¶$nic, Fabaceae, Phaseolus vulgaris, Lectine, $TOXPROT, Toxicite, Binding, Intestin, Graine, Histopathologie, Coleoptera, Bruchidae, Callosobruchus maculatus, RPI, RŽsistance, insecte4D, Yvan [3691]‘Gatehouse, A.M.R. 1986 Mini-symposium on lectins B7Gatehouse, A.M.R. Minney, B.H.P. Dobie, P. Hilder, V.A. 1990^XBiochemical resistance to bruchid attack in legume seeds: investigation and exploitation>8Bruchids and Legumes: Economics, Ecology and Coevolution Dordrecht (NDL) b\Fujii, K., Gatehouse, A.M.R., Johnso, C.D., Mitchel, R., Yoshida, T., Ed¡ Kluwer Acad. Publ.241-256h 36604Dnh$TOXPROT, RPI, RŽsistance, Fabaceae, Coleoptera, Bruchidae, Revue, insecte, lectine, inhibiteur proteaseNHGatehouse, A.M.R. Howe, D.S. Flemming, J.E. Hilder, V.A. Gatehouse, J.A. 1991žYBiochemical basis of insect resistance in winged bean (Psophocarpus tetragonolobus) seeds7 7 R J. Sci. Food Agric. 55 63-744.Journal of the Science of Food and Agriculture 3656°ªRPI, RŽsistance, Fabaceae, Graine, Psophocarpus tetragonolobus, Coleoptera, Bruchidae, Callosobruchus maculatus, Lectine, $TOXPROT, Toxicite, Inhibiteur protease, insecte4DYJXxWÚVºT®URSvRQ¢P<O¢IzMHHzJJDGatehouse, A.M.R. Hilder, V.A. Powel, K. Boulter, D. Gatehouse, J.A. 1992b[Potential of plant-derived genes in the genetic manipulation of crops for insect resistanceÌ6/Proc. 8th Int. Symp. Insect-Plant Relationships Dordrecht (NDL) HAS.B.J. Menken, J.H. Visser & P. Harrewijn, Ed¡ Kluwer Acad. Publ.221-234 3403ª£$nic, $TOXPROT, Lectine, Inhibiteur protease, Genie genetique, Revue, RŽsistance, Transgenose, Lepidoptera, Orthoptera, Coleoptera, Homoptera, WGA, insecte, plante2,Gatehouse, A.M.R. Down, R.E. Gatehouse, J.A. 1995’ŒTransgenic potato plants expressing snowdrop lectin show enhanced resistance to homopteran and lepidopteran insect pests in glasshouse trialD>Gordon Research Conference in Agricultural Sciences. Feb 5-10. ,&CASA SIRENA RESORT, Oxmard, CaliforniaNi 0145¦ puceron, Aulacorthum solani, lectine, mode d'action, GNA, Galanthus nivalis, Nilaparvata lugens, croissance , fecondite, transgenose, poster, Lacanobia oleracea†Gordon Research Conference in Agricultural Sciences. Chemical/biological synergies to reduce inputs for pest control. Feb 5-10.TNGatehouse, A.M.R. Powell, K.S. Peumans, W.J. van Damme, E.J.M. Gatehouse, J.A. 1995TMInsecticidal properties of plant lectins: their potential in plant protectionð Pusztai, A. & Bardocz, S.d& Lectins, Biomedical perspectives London Francis & Taylor Ltd 35-57 Ni 0293›plante, rŽsistance, lectine, insecte, $toxprot, homoptere,revue, lepidoptere, coleoptere, WGA, Empoasca fabae, PHA, ConA, Acyrthosiphon pisum, GNA, Galanthus, Concanavaline, Lucilia cuprina, mode d'action, Heliothis virescens, Callosobruchus maculatus, transgenese(!Gatehouse, A.M.R. Gatehouse, J.A.› 1998zsIdentifying proteins with insecticidal activity: Use of encoding genes to produce insect-resistant transgenic crops  Pestic. Sci.522`165-175 Pesticides Science„}Revue, Coleoptera, Lepidoptera, Homoptera, Proteine, Inhibiteur enzyme, Inhibiteur protease, Lectine, Resistance, Transgenoseª"Girousse, C. Bournoville, R. 199470227-235 4444voRole of phloem sap quality and exudation characteristics on performance of pea aphid grown on lucerne genotypesn–$phloem, Homoptera, Aphididae, Acyrthosiphon pisum, Medicago sativa, rŽsistance, insecte, antibiose, stylectomie, amino acides, sucre, exudation.'Entomologia experimentalis et applicatanEntomol. exp. appl.e Grant, G.  1991Lectins 6/Eds D'Mello, J.P.F.; Duffus C.M. & Duffus, J.H.€&Toxic substances in crop plants  Cambridge $The Royal Society of Chemistry 49-67 3496:4$toxprot, revue, lectine, insecte, Con A, gŽnŽralitŽ2+bibliothque labo SO24 chapitre photocopiŽ "Grant, G. van Driessche, E. 1993@:Legume lectins : physiochemical and nutritional properties :3Eds van der Poel, A.F.B.; Huisman, J. & Saini, H.S.XQSecond International Workshop on "Antinutritional factors (ANFs) in legume seeds" 0)Wageningen, The Netherlands, 1-3 dec.1993¸219-234Ni 0274 4-lectine, insecte, legume, plante, rŽsistance,ì"bouquin disponible ˆ NanteseGroeters, F.R. 1995Insecticide resistanceTrend Ecol. Evolut.  Ed¡ Elsevier104 164 $Trends in Ecology & Evolution 0169-5347>8Letter FR Groeters, 172 Lapla Rd, Kingston, NY 12401 USA SƒLECTIONA.'Gurevitz, M. Zlotkin, E. Zilberberg, N.T 1990š”Characterization of the Transcript for a Depressant Insect Selective Neurotoxin Gene with an Isolated cDNA Clone from the Scorpion Buthotus-Judaicus FEBS Letters 2692229-232nhToxine, Neurotoxicite, Insecta, Scorpionidae, ADNc, PCR, Sequence, Expression tissu specifique, $TOXPROT 1978*$Habibi, J. Backus, E.A. Czapla, T.H. 1993VPPlant lectins affect survival of the potato leafhopper (Homoptera: Cicadellidae)J. Econ. Entomo.863Ž945-951h$Journal of Economic Entomology 3723ZTlectin; $toxprot; cicadelle; artificial diet; Empoasca fabae; PHA; WGA; Phaseolus vulgaris; Phaseolus limensis; Lens culinaris; Pisum sativum; Arachis hypogaea; Dolichos bifloris; Glycine max, Griffonia simplicifolia, Bauhinia purpurea, Triticum vulgaris (WGA), Artocarpus integrifolia, Codium fragile, Amaranthus caudatus, lectine, insecte JIPŽ*$Habibi, J. Backus, E.A. Czapla, T.C. 1998Ü—Subcellular effects and localisation of binding sites of phytohemagglutinin in the potato leafhopper, Empoasca fabae (Insecta: Homoptera: Cicadellidae)H f t Cell and Tissue Research 294›561-571Cell and Tissue Research ˆ rechercher,&lectine, mode d'action, PHA, Hemiptera JIP,%Habibi, J. Backus, E.A. Huesing, J.E.Œ 2000ð«Effects of phytohemagglutinin (PHA) on the structure of midgut epithelial cells and localization of its bindinfg sites in western tarnished plant bug Lygus hesperus Knight – ¤ "Journal of Insect Physiology46611-619 "Journal of Insect PhysiologyNi&lectine, mode d'action, insecteð JIP>8Harper, S.M. Crenshaw, R.W. Mullins, M.A. Privalle, L.S. 19956/Lectin binding to insect brush border membranesÐJ. Econ. Entomol. *#9301 Annapolis Rd, Lanham, MD 20706‹ Entomol Soc Amer885_ 1197-1202$Journal of Economic Entomology 0022-0493PNi 0564ìåwestern corn rootworm; lectine; SOUTHERN CORN-ROOTWORM; CHRYSOMELIDAE; COLEOPTERA, interaction, brush border membranes, BBM, Ostrinia nubilalis, Biabrotica virgifera virgifera, binding, European corn borer, lectine, mode d'actionTNIt has been hypothesized that plant lectins play a role in the defense of the plant from fungal and insect attack. Several insects species have been shown to be sensitive to lectins. However, the mechanism by which lectins exert their insecticidal activity is unknown. The results presented in this article compare the insecticidal activity of lectins with their apparent ability to bind to brush border membrane proteins of European corn borer, Ostrinia nubilalis Hubner, and Western corn rootworm, Diabrotica virgifera virgifera Le-Conte. Lectins that caused significant mortality or a decrease in weight gain in O. nubilalis also bound strongly to O. nubilalis brush border membrane proteins, but not all lectins that bound strongly were insecticidal. Relationships between binding and mortality were less consistent in D, virgifera virgifera.`YJIP Article SM Harper, Ciba Biotechnol, Insect Control Grp, Res Triangle Pk, NC 27709 USAüHeinrichs, E.A.! 1992XQRice insects : the role of host plant resistance in integrated management systemsÿKoren J. Appl. Entomol.313256-275Ni 0412ï´®lutte intŽgrŽe, plante resistante, insecte, IPM , Integrated Pest Management, gestion rŽsistance, Nephotettix virescens, Nilaparvata lugens, riz, lutte biologique, sŽlection,Heinrichs, E.A.ÿ 1994<5Development of multiple pest resistant crop cultivars.J. Agr. Entomol.113225-253 ("Journal of Agricultural EntomologyNi 0413TNArticle EA Heinrichs, W Africa Rice Dev Assoc, 01 BP 2551, Bouake, Cote Ivoire.'crop cultivars; insecte; multiple pest rŽsistance; nematodes; sŽlection; maladie; Homopteres, DELPHACIDAE; INSECTICIDES, lutte intŽgrŽe, plante resistante, insecte, IPM , Integrated Pest Management, gestion rŽsistance, Nephotettix virescens, Nilaparvata lugens, riz, lutte biologique, sŽlection,e ŒXEXTATOSOMA-TIARATUMTA FECUNDITYfeeding behavior Feeding Behavior ModificationFEEDING INSECTSYEFIELDFIELD POPULATIONSFlight Muscle BreakdownËð FLUORESCENCESfluorescent brightenerar FLYOLFOREST TENT CATERPILLAREP G-oquakalGEL-ELECTROPHORESISINgene expressionns¨¢GENE, plante transgenique, insecte, bruche , rŽsistance , plante, transgenese, Brochus pisorum, Pisum sativum, Phaseolus vulgaris, inhibiteur protease, promoteur, 0 GENETIC-BASIS GENETICSNd_genetique des population, sŽlection, population, evolution, adaptation, revue, concept, insecteª°LIgenetique des populations, insecte, sŽlection, adaptation, consanguinite,|wgŽnŽtique quantitative, equilibre Hardy-Weinberg, insecte, population, revue, concept, sŽlection, adaptation, evolution¦0 GLOSSINAT("GLOVER, puceron, aphid, Isoenzymes¤ Glycine max, Griffonia simplicifolia, Bauhinia purpurea, Triticum vulgaris (WGA), Artocarpus integrifolia, Codium fragile, Amaranthus caudatus, lectine, insecte° GLYPHOSATEONS$!GNA, lectine, insecte, agglutinin GNA, mode d'action, insecte,Graminella nigrifronsGranulated CellslGUS, Galanthus nivalisnsgGUTTE gut contentsvGut Endocrine Cells ¤ŸGUT, intestin, Trypanosoma congolense, Glossina palpalis palpalis, Trypanosoma brucei rhodesiense, Glossina pallidipes, midgut, insecte, mode d'action, binding~p H+-ATPASEHEATOHELIOTHIS VIRESCENSEPHELIOTHIS-VIRESCENSPT Hemiptera HEMOCYTES HEMOLYMPH<6HEMOLYMPH, mode d'action, binding, recepteur, mannose,WË° HEMOLYMPHEes $ HEMOLYMPHe, Sarcophaga peregrinaG HeptenophosPr HERBIVORESNIO Heteroptera histopathologyigh HOMOPTERAHomoptera, Aphididae(ÔÑHomoptera, aphididae, bird cherry-oat aphid (Rhopalosiphum padi L.) , blŽ, wheat, sŽlection, insecte, trichome, rŽsistance, plante, sŽlection, cereal leaf beetle (Coleoptera: Chrysomelidae), Oulema melanopus,lfHomoptera, Aphididae, Acyrthosiphon pisum, Fabaceae, Medicago sativa, RPI, RŽsistance, Lutte varietaleWËЊHomoptera, Aphididae, Delphacidae, $TOXPROT, Lectine, Transgenose, Lutte varietale, Brevet, Toxicite, rŽsistance, puceron, lutte intŽgrŽe,D0,Homoptera, Aphididae, EPG, Piqure, IngestionptoHomoptera, Aphididae, Lectine,Peptidase, Miellat, Toxicite, $TOXPROT, insecte, $lectin, mode d'action, binding,ˆPLHomoptera, Aphididae, Myzus persicae, Rosaceae, Arbre, RPI, Hypersensibilite(hcHomoptera, Aphididae, Myzus persicae, Rosaceae, Arbre, RPI, RŽsistance, Specificite, Virus, VectionϘtpHomoptera, aphididae, RŽsistance, bird cherry-oat aphid (Rhopalosiphum padi L.) , bŽ, wheat, sŽlection, insecte, ýHomoptera, aphididae, rŽsistance, plante, insecte, puceron, sŽlection, mecanisme de la rŽsistance, EPG, RPI, physiologie, biochimie, analyse multivariŽe, ACP, AFC, antiappŽtent, phagostimulant, acide hydroxamique, DIMBOA, acide aminŽ, sve, phlome, calPJHomoptera, Laser YAG, Phloeme, Stylectomie, $PHLOEM, Poaceae, Oryza sativa;pHomopteres, DELPHACIDAEe HOP, rŽsistance, puceron HOSTS HOST PLANT Host Plant Preferencehost plant rŽsistanceHOST SPECIFICITYEhost-plant rŽsistanceHOSTS, midgut,ENE HUMAN-IMMUNODEFICIENCY-VIRUSHYALOPHORA CECROPIAINimmune structures$immunite, anticorps monoclonaux immunocytochimierImmunohistologieDIMMUNOREACTIVITYLin vitro rearingtinduced action potentialPLInhibiteur protease, Glycine max, Fabaceae, Dosage, Graine, lectine, insecteœ˜Inhibiteur protease, insecte, Amylase, Lectine, RŽsistance, Fabaceae, Phaseolus vulgaris, Coleoptera, Bruchidae, Callosobruchus maculatus, RPI, $TOXPROT+`\Inhibiteur protease, Lycopersicon, Fruit, Genie genetique, Electrophorese, SDS-PAGE, insecte¬¨Inhibiteur protease, RŽsistance, Vigna unguiculata, Callosobruchus maculatus, Lectine, Tannin, Zabrotes subfasciatus, Phaseolus vulgaris, Coleoptera, Bruchidae, insecte Insectlat Insect AttackINSECT EPITHELIAPinsect immunity insect rŽsistance insecta}j ihhLgDf6eÞdc(bÜaÀ`V_^F]\b[(Z€.'Herper, S.M. Hopkins, T.L. Czapla, T.H.` 1998̈Effect of wheat germ agglutinin on formation and sructure of the peritrophic membrane in European corn borer (Ostrinia nubilalis) larave n € Tissue and Cell 30166-176ŽTissue and Cell›Ni&mode d'action, lectine, insecte JIPp$Hilder, V.A. Gatehouse, A.M.Rd 1990HATransforming plants as a means of crop protection against insectsOutlook on Agriculture193179-183 4285, Niha$toxprot, transgenose, insecte, rŽsistance, CpTI, IP, inhibiteur protease, revue, plante, lectine>7Hilder, V.A. Gatehouse, A.M.R. Powell, K.S. Boulter, D. 1993 1-49 Brevet 4503hbProteins with insecticidal properties against homopteran insects and their use in plant protectionŠHomoptera, Aphididae, Delphacidae, $TOXPROT, Lectine, Transgenose, Lutte varietale, Brevet, Toxicite, rŽsistance, puceron, lutte intŽgrŽe, Hoshizaki, S.d 1994ÒŽDetection of isozyme polymorphism and estimation of geographic variation in the brown planthopper, Nilaparvata lugens (Homoptera: Delphacidae) c u  Bul. Entomol.84503-508 &Bulletin Entomological research Ni 1081Œ¬¥Nilaparvata lugens, isozyme, polymorphisme, enzyme, population, migration, isoelectic focusing (IEF), Žlectrophorse, insecticide, rŽsistance, Homoptera, Delphacidae $Lydia("Houk, E.J. Arcus, Y.M. Hardy, J.L. 1986$Arch. Insect Biochem. Physiol.3135-1464.Archives of Insect Biochemiqtry and PhysiologyNi 0101>7estomac, BBM, brush border, ME, insecte, electrophorese,XRIsolation and characterization of brush border fragments from mosquito mesenterons Huesing, J.E.d 199182Lectins as plant chemical defenses against insects Purdue University  PhD 4024, Ni 0991:ö$toxprot, plant lectin, insecte, rŽsistance, milieu artificiel, Callosobruchus maculatus, cowpea weevil, osage orange lectin, peanut agglutinin, N-acetylgalactosamine, GalNAc, N-acetylglucosamine,GlcNAc, wheat germ (WGA), rice (RL), tomato (TL), jimson weed (DSA), stinging nettle(UDA), binding, toxicite, chitin-binding protein, midgut, intestin, histopathologie, lesion, survie, fecondite, physiologie, transgenose, PHA, phytohemagglutinin, a-amylase inhibitor, lectine, insecte, Con A, mode d'action » ¼ >8Order number DA9132460 Major professor: Larry L. Murdock.'Huesing, J.E. Murdock, L.L. Shade, R.E. 1991Phytochemistry30785-788Phytochemistry 2235zs$TOXPROT, Lectine, Coleoptera, Developpement larvaire, Bruchidae, Callosobruchus maculatus, Toxicite, HPLC, insecteˆ importŽ de 4DôF?Effect of Wheat Germ Isolectins on development of Cowpea Weevilô.'Huesing, J.E. Murdock, L.L. Shade, R.E. 1991Phytochemistry3011 3565-3568Phytochemistry 3000 importŽ de 4Dø^XRice and stinging nettle lectins: insecticidal activity similar to wheat germ agglutinin»$TOXPROT, Lectine, Urtica dioica, Oryza sativa, Poaceae, Coleoptera, Bruchidae, Callosobruchus maculatus, Amylase, Inhibiteur protease, Croissance, Toxicite, RŽsistance, RPI, WGA, insecten>8Huesing, J.E. Shade, R.E. Chrispeels, M.J. Murdock, L.L. 1991Plant Physiol.96993-996ºPlant Physiology 2516 importŽ de 4Dø–fa-amylase inhibitor, not phytohemagglutinin, explains resistance of common bean seeds to Cowpea Weevil  ž˜Inhibiteur protease, insecte, Amylase, Lectine, RŽsistance, Fabaceae, Phaseolus vulgaris, Coleoptera, Bruchidae, Callosobruchus maculatus, RPI, $TOXPROT("Hwang, D.L. Yang, W.K. Foard, D.E. 1978Plant Physiol.61 30-34 1947RLInhibiteur protease, Glycine max, Fabaceae, Dosage, Graine, lectine, insectepiRapid release of protease inhibitors from soybeans Immunochemical quantitation and parallels with lectinscHypsa, V. Grubhoffer, L. 1995xrAn LPS-binding hemagglutinin in the midgut of triatoma infestans: partial characterization and tissue localization"Arch Insect Biochem Physioly4.Archives of Insect Biochemistry and Physiology HADiv John Wiley & Sons Inc, 605 Third Ave, New York, NY 10158-0012t  Wiley-Liss283D247-255i 0739-4462Tˆlectin; agglutination; lipopolysaccharide; PERITROPHIC MEMBRANE; LECTIN; HEMOLYMPH; PURIFICATION; GLOSSINA; PROTEIN; DIPTERA; GUTs A hemagglutinin was identified and partially characterized in the crop of the bug Triatoma infestans. It agglutinated mouse and rabbit erythrocytes, and was strongly inhibited by bacterial lipopolysaccharides. SDS-PAGE and immunoblotting with specific antibodies identified a dominant protein with molecular mass of 20 kDa under reducing conditions. The protein seems to be synthesized in the crop epithelial cells and deposited on the inner crop surface. Its possible biological role is discussed. (C) 1995 Wiley-Liss, Inc.xrArticle V Hypsa, Acad Sci Czech Republ, Inst Parasitol, Branisovska 31, CR-37005 Ceske Budejovice,, Czech Republic Jacquard, A. 1977,%Concepts en gŽnŽtique des populations  Jacquard, A. Paris MassonLabo INSA-Lyon #B53&PIgenetique des populations, insecte, sŽlection, adaptation, consanguinite,&JaffŽ, W.G. Seidl, D.S.Ü 1992"Toxicology of plant lectinsFood Poisoning New York Ed¡ Marcel Dekkerÿ7263-290 Handbook of Natural Toxins 4199¢$toxprot, lectine, mode d'action, phytohemagglutinin, PHA, castor bean, Ricinus communis, ricin, jeriquinty, Abrus precatorus, plante, binding, recepteur, insecte H X m } b\Article WG Jaffe, Cent Univ Venezuela, Fac Sci, Sch Biol, Dept Cell Biol, Caracas, Venezuela Janzen, D.H. Juster, H.B.  1976VPInsecticidal action of the phytohemagglutinin in Black Beans on a bruchid beetleScience 192795-796›Science 3561„}lectine, Phaseolus vulgaris, $toxprot, Callosobruchus maculatus, Vigna unguiculata, trypsin inhibitor, insecte, mode d'action06/Janzen, D.H. Ryan, C.A. Liener, I.E. Pearce, G. 1986ZTPotentially defensive proteins in mature seeds of 59 species of tropical leguminosae"Journal of Chemical Ecology\126T 1469-1480\Ni 0701 `Zlectine, plante, rŽsistance, legumineuse, inhibiteur protease, defense, insecte, predateur Jermy, T. 1993LEEvolution of insect-plant relationships - a devil's advocate approach661, 3-12 3631`YReview T Jermy, Hungarian Acad Sci, Inst Plant Protect, POB 102, H-1525 Budapest, Hungary4.Evolution; Coevolution; SŽlection; Insect Attack; Plant Defense; Competition; Enemy Free Space; Chemoreception; Specialization; Plant Recognition; PHYTOPHAGOUS INSECTS; HOST SPECIFICITY; FEEDING INSECTS; SPECIALIZATION; COEVOLUTION; COMPETITION; HERBIVORES; PREDATION; ASSOCIATIONS; REPRODUCTION, revue.'Entomologia experimentalis et applicataeEntomol. exp. appl.eF@Jiang, B. Siregar, U. Willeford, K.O. Luthe, D.S. Williams, W.P. 1995€zAssociation of a 33-kilodalton cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growthPlant Physiol. 108  1631-1640ÐNi 1194 rŽsistance, insecte, mais, sŽlection, mecanisme, RPI, Zea mays, Spodoptera frugiperda, Diatraea grandiosella, test, biochimie, proteine, purification, milieu artificiel, electrophorese 2D, genotype, cysteine, immunomarquage, immunoblot, proteinase, sequencage, biomol, œÙLaukkanen, M.L.¦l Launis, K.( Law, J.H.Le Boulc'h, V.Цl Lee, H.I. Leitch, B.( Lemos, F.J.A. Lepier, A.( Levine, E.B.( Lewis, K. Liener, I.E.(0+Liener, I.E. ; Sharon, N. ; Goldstein, I.J.Ñ Liljegren, D.Lindquist, R.K.¦l Lis, H.Îà Lun, Y.J. Luo, K.Îà Luthe, D.S.(Mac Gaughey, W.H.Maccutchen, B.F.lMacedo, M.L.R.Цl Maddox, D.( Maddox, D.W.( Maeda, S. Main, C.A.( Maison, P.( Maris, G.C.( Marsh, J.Martinez-Ramirez, A.C.›– Masson, L.H Massonie, G.( Maudlin, I.( Mazza, A. McCall, P.J.(McCutchen, B.F.¦lMcgregor, P.G.ЦlMckenzie, J.A.Цl McManus, M.( McPherson, K. Meeusen, R.L. Meghji, M.R.( Meik, J.àMenancio-Hautea, D.›” Merlin, E.(Mesterhazy, A.Цl Miller, J.R. Miller & T.A. üT Milner, R.J.(Minney, B.H.P.ЦlMolyneux, D.H.Цl Monet, R. Monties, B.( Moore, A. Moran, N.A.( Morhy, L. Morrot, G.( Mourey, L.( Mullins, M.A.Munsterman, E.Цl Murdock, L.L.($Myers., John A. Thomas and Laurie A.€4/N.H. Battey, H.G. Dickinson & A.M. Hetherington Nardon, C.(Narvaez-Vasquez, J.›” Natori, S.( Nault, L.R.( Neet, K.E.( Newby, R.C.( Nielsen, S.S. Nobel, P.S.( Oatman, E.R.( Okerblom, C.( Ollivier, L.(Orozco-Cardenas, M.L. Osborn, T.C.( Owen, W.G.( Pages, C. Palekar, N.( Panayotov, I. Papp, M.àPathak, J.P.N.Цl Pavlova, S.( Pearce, G.( Pearson, R.D.Pedelacq, J.D.ЦlPennacchio, F.ЦlPereira, M.E.A.¦lPeres Silva, C.¦l Perring, T.M.0+Peters, D.C., Webster, J.A., Chlouber, C.S.Ñ Peumans, W.J.Pham-Delgue, M.-H.›” Pickett, J.A. Piron, P.G.M. 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Sun, S.S.Sutherland, P.W.lTabashnik, B.E.¦l Tabe, L.M.( Tadmor, U.( Talekar, N.S. Tellam, R.L.( Thi Loc, N.( Timm, D.E.(Tjallingii, W.F.lTompkins, G.J.Цl Toscano, N.C. Tremblay, E.( Trumble, J.T. van Damme, E. van Damme, E., Peumans, W. üTvan Damme, E.J.M.van der Meijden, E.›”van der Salm, T.lvan Driessche, E.van Emden, H.F.¦lvan Heusden, M.C.Vandamme, E.J.M.l Verbeke, M.( Visser, B.( Visser, J.H.( Volkov, A.G.( Volrath, S.L.Vondohlen, C.D.¦l Vuocolo, T.( Wadhams, L.J. Wallace, B.( Wang, M.B.( Wang, N.à Warren, G.( Warren, G.W.(Wayadande, A.C.¦l Wehner, T.C.( Welburn, S.C. Wieczorek, H.Wilkinson, T.L.¦lWilleford, K.O.¦l Williams, S.(Williams, W.P.Цl Wiseman, B.R. Wolff, K.Woodcock, C.M.ЦlWoodhouse, S.D.¦l Wright, M.(Xavierfilho, J.¦l Yan, F.S. Yang, W.K.( Young, N.D.( Ziegler, R.(Zilberberg, N.Цl Zlotkin, E.(  äoLFArcelin, Lectine, Phaseolus vulgaris, Graine, Binding, OligosaccharideWËÐ ARCELINeSARMIGERA LEPIDOPTERAT AROA GENEartificial dietartificial dietst ASSOCIATIONSO attractants³$b-glucuronidasetsBacillus thuringiensis! BACILLUS-THURINGIENSISUSSbacterial injectionseBACTERICIDAL PROTEINN BACULOVIRUSES@;BBMV, intestin, recepteur, mode d'action, lectine, manduca,ÀX BEHAVIORE BINDING-SITES BIOLOGYONBIOMPHALARIA-GLABRATA BOMBYX-MORIESBRAINBrassica fruticulosa(Brassica spinescensa(BRASSICA-OLERACEABREEDING LINESGUALGBrevet, $TOXPROT, Lectine, Insecticide, Lysine, insecte, lutte intŽgrŽeË \XBrevet, Lectine, Champignon, $TOXPROT, Insecticide, Fongicide, Transgenose, WGA, puceronÀdaBrevet, Patatine, Esterase, $TOXPROT, Toxicite, Lepidoptera, Solanum tuberosum, lectine, insecte,Brevicoryne brassicaeBRUSH-BORDER MEMBRANEBtcep Buchnerai BUTTERFLY PIERIS-BRASSICAEXINCALLOSOBRUCHUS-MACULATUSS calyx fluidalCamv-35S PromoterCARDIOCHILES NIGRICEPSion Castnia LicusCELL-SURFACE CHANGESe CEREUS }ˆƒCharacterisation , purification, recepteur,Bacillus thuringiensis, d-endotoxin, mode d'action, insecte, WGA, lectine, SBA, binding| chemical injury Chemoreceptionce chitinlan chitinaseCHLOROTIC DWARF VIRUS Chrysanthemum CHRYSOMELIDAE cicadelle CICADELLIDAES coagulation  Coevolution³$¨¢Coleoptera, $TOXPROT, Inhibiteur protease, Trypsine, Fabaceae, RPI, RŽsistance, Vigna unguiculata, Bruchidae, Callosobruchus maculatus, Toxicite, lectine, insecte 0`]Coleoptera, Bruchidae, Heteroside, Fabaceae, Phaseolus vulgaris, RŽsistance, Lectine, insecte Coleoptera, Bruchidae, Phaseolus vulgaris, Fabaceae, RPI, RŽsistance, Glucide, Lectine, Heteroside, Fucose, Arabinose, Toxicite, Antibiose, $TOXPROT, insecte°¬Coleoptera, Chrysomelidae, Lectine, $TOXPROT, Developpement larvaire, Lepidoptera, Pyralidae, Ostrinia nubilalis, RPI, RŽsistance, Toxicite, mode d'action, insecte, binding¤žCOLEOPTERA, interaction, brush border membranes, BBM, Ostrinia nubilalis, Biabrotica virgifera virgifera, binding, European corn borer, lectine, mode d'action-Œ@ýColeoptera, Lepidoptera, Toxine, $TOXPROT, Cytolyse, Cytotoxicite,Enterolobium contortisiliquum, enterolobin, insect toxicity, Callosobruchus maculatus, Spodoptera littoralis, mode d'action, intestin, microvilli, ME, microscopie electronique, epithelium collection, insecte, aphideCOLORADO BEETLECE Competitionse COMPONENTSUS-concanavalin A! CONCANAVALIN-ARTP COTTON APHIDOCOWPEA VIGNA-UNGUICULATAO COWPEA WEEVILcrop cultivarscrystal proteingiCRYSTAL PROTEIN GENES Cucumberi CULICIDAE<6CULTIVARS, lutte intŽgrŽe, insecte, rŽsistance, planteWË°culture IN VITROEDalbulus maidisxf DEFENSESM0,DEFENSE, mode d'action, inhibiteur protease, DELPHACIDAEDODELTA-ENDOTOXINOL DELTAMETHRINVÜ×Dendrathema grandiflora, Frankliniella occidentalis, Thysanoptera, Thripidae, Oviposition preference, feeding damage, mode d'action, mŽcanisme rŽsistance, RPI, test de choix, screening, sŽlection variŽtale, insecte,ÌP DETERMINANTSS DIAMONDBACK MOTH LEPIDOPTERA DiazinonrDIGESTIVE PHYSIOLOGYI digestive protease activity–x DIPTERAAT DIVERSITY, aphide, phylogenieDNAntDolichos bifloris DROSOPHILA-TIECONOMIC INJURY LEVELSERAELDERBERRY SAMBUCUS-NIGRA electro-antennographie (EAG)Pelectronic monitoring Electronic Monitoring SystemP$electronique microscopie , METedrelectrophorese 2DElectrophoresisis EMBRYOGENESISEmpoasca fabaetEncarsia aurantiiEnemy Free SpaceENZYME-ACTIVITIES<7estomac, BBM, brush border, ME, insecte, electrophoreseË°("ETHYL METHANESULFONATE MUTAGENESIS-0 EvolutionpmEvolution, comportement, polymorphisme, genetique quantitative, Choristoneura rosaceana (Family: Tortricidae)EVOLUTIONARY TREESE  EXPRESSIONVULœ˜EXPRESSION, lectin, Eranthis hyemalis, (Winter aconite), inhibiteur de la synthese proteique, inhibitor of protein synthesis, $toxprot, lectine, insecteµ¶·¶¶¶µµ¶´´¶¹·´µµ´µµ´·¶¶·¶¶¶¶³³µ·¸¸¶µ´µ·¶¶¶·¹¶´µµµ¶µ¶µ´´¶·¶¶µµ´³µ¸¸µ³³´³³µ´²³´´´µ¶µ¶¶·¶µµ¶´´´²³µ³´´³³²±°±°±³³²²²³´´³³³²±²²²³´´³²±³´´³³³µ´²²²²±±±²´³³²±±²°±±±²²±±°±±±°±°°³²¯®°±¯¯®°¯­¯°±°¬¯°°°¯®¯°®°°®­®®®°¯®°¯­®¯°°±°¯°¯²°°¯¯®¯±°¯°®®°°²¯¯°±¯°±°®­°¯¯°¯«¬­­­­®®®µµ¶···¶¶¶¶¶·¸µ³µµµµ¶´¶µ¶·¶··µ²³¶¶···¶´µ·¶µ´·¹µ´¶µµ¶µµ³³´¶·¶µ´³³³µ¶µ²²³³±°³³³²²´´³µµµ´¶¶µ·¶²²´´µ·´´³³³²²°³¯°±²²³µ³´´´³²±¯¯°²´´´´³±³´´³²±³´²²±±°±±²´´´²±²³±²±°°°¯°°±²±±°°±¯¯®®°±¯®±²¯¬¯±±°­±¯¬®¯®¯°®°°¯®®®±²¯®°°®®¯±±²±®°°±®®¯°¯®°­®±®®±­­®®®¯®±²°­¬®¯¯­¬®­­«¬¬­­¬µ·¸¸¸¸¸¶¶¶¶··µµµµ¶··¶µµ·¹¸¸¸¶··³¶¶¶¶·¶´µ´´´´µ¶···¶µµµµµ·µ´¶¶µµµ³µ²±³³´µ¶µ´´³³³³²°²´µ´´¶´´³²³¶´´µµ±´³²±¯±±²´³±³¶µ´µ´´³³°®®±²±µ´³³²±²³´²²³´²°°±±±²´²³³±±²³³²°°°²²°°°°³³°°²°¯®­¯°¯°±±°°°±°°°¯­­¯±±°®°¯¯¯¯¯¯°´¯¯±°°°¯¯°±²²±±²±°±°¯°¯¯¯±¯°´°°´±¯²°®¯­¯¯²¯®¯­®«¬­®¯®®¯µ¶·¸¸¸·µµµ¶¸·´³´¸¸¸···¶¸·¸¸¸··¶µ´´µµ¶¶µµµµµµµ¶¶··¶µµµµ´µµµ··µµ¶´´´³³³µ··¶µ´³²²³³³´µµ´´µ³µµ³´µ´´µ³±³³²±±´²²´´²³µ´³´´´´³±°®±²²³³²³³³´³²±²³±°°²±±²³´±²²±±²³²²±±±²²°°°¯±²²²²°°°°±°¯¯°¯¯®°±°¯±°®®°±°¯­¯¯°°±¯®«¯­®¯¯°°¯°±±³³²²²±°°°¯¯®°¯¯®±¶³²²²°±¯­¯±±°±¯®¯­®«¬­®¯­­­ (\ RƒSISTANCEIVIrŽsistance managementXSrŽsistance plante, gestion rŽsistance, variabilite, insecte, sŽlection, variabilite–xpjrŽsistance, cucurbitaceae, insectes, Cucumis, genetique, sŽlection, revue, puceron, melon, lutte intŽgrŽe, | ýrŽsistance, insecte, mais, sŽlection, mecanisme, RPI, Zea mays, Spodoptera frugiperda, Diatraea grandiosella, test, biochimie, proteine, purification, milieu artificiel, electrophorese 2D, genotype, cysteine, immunomarquage, immunoblot, proteinase, sequ0,rŽsistance, plante, insecte, COLORADO BEETLE‘TNrŽsistance, plante, insecte, ecologie, revue, evolution, genetique, sŽlection,,7‹rŽsistance,Liriomyza trifolii (Burgess), melon (Cucumis melo L.), diptere, tomate, sŽlection, mecanisme rŽsistance, insecte, cucurbitacees,DRIBOSOMAL-RNA GENES ¨£Ribosome, Toxine, $TOXPROT, Lectine, Proteine RIP, Musca domestica, Toxicite, Diptera, Phenylalanine, Traduction, Glycosidase, Saporine, Ricine, Eucaryote, insecte 0$ rice sucrose synthase-1 promoter RICE VARIETIESPER RICE, WGARICINRNATERNA TRANSCRIPTS GRPI, antibiosence°ªRPI, RŽsistance, Fabaceae, Graine, Psophocarpus tetragonolobus, Coleoptera, Bruchidae, Callosobruchus maculatus, Lectine, $TOXPROT, Toxicite, Inhibiteur protease, insecte!  Salix sericeaSAMPLING PLANSGUA SANDFLY LUTZOMYIA LONGIPALPISSARCOPHAGA LECTIN GENEect SARCOTOXIN-IE4.sauvion, rahbŽ, transgenese, lectine, puceron,-ƒpˆƒSchizaphis graminum, Electrophoresis, Esterase, Isozymes, insecticide, rŽsistance, Žlectrophorse, polymorphisme, PAGE, Isoenzymes–xSCHIZAPHIS-GRAMINUMdiSECONDARY STRUCTURE SEEDSSELECTIVE CHANNELSNSISELECTIVE MORTALITYAT semiochimique SEQUENCEL SEQUENCES SƒLECTIONtnsŽlection , plante, rŽsistance, insecte, revue, virus, bacterie, mecanisme de la rŽsistance, concept, biotype,-„@hbsŽlection, rŽsistance, plante, insecte, QTL, retrocroisement, sŽlection reccurente, RFLP, marqueur |  Sheep BlowflySITE, pheromone, insecte,ÈÃsnowdrop lectin, GNA, artificial diet, transgenic plant, Eulophus pennicornis, Hymenoptera, Eulophidae, parasitoid, tomato moth, Lacanobia oleracea, Lepidoptera, Noctuidea, mode d'action, lectine 0SOIL, midgut, pHs„€Solanaceae, Proteine, Inhibiteur protease, Transgenose, Amylase, Graine, RPI, Coleoptera, RŽsistance, Lectine, $TOXPROT, insecteSORGHUM MIDGE DIPTERASOUTHERN CORN-ROOTWORMWÔ Specializationce SPECIFICITYAKSpodoptera exiguaSPODOPTERA-EXIGUAD@Stylectomie, Revue, Homoptera, Xyleme, $PHLOEM, Calcium, MiellatSUBSP KURSTAKIMCE SUBUNITWESURFACE-PLASMON RESONANCE SWEET-POTATOE symbioseisymbiose, ENDOSYMBIONTionSYNTHETIC ATTRACTANTHTeleogryllus commodus teratocytesal$THURINGIENSIS DELTA-ENDOTOXINSWÔ TOBACCOeSTOBACCO BUDWORMCE TOLERANCE TOMATO PLANTStomato, aleurodes˜’Toxicite, Lectine, Insecticide, Fabaceae, Phaseolus vulgaris, Coleoptera, Bruchidae, RPI, Defense, $TOXPROT, insecte, arceline, rŽsistance, plantelhToxine, Neurotoxicite, Insecta, Scorpionidae, ADNc, PCR, Sequence, Expression tissu specifique, $TOXPROTÐTransgenic Plants,)transgenic plants, transgenose, promoteurTRANSGENIC TOBACCO PLANTSd^transgenose, insecte, puceron, rŽsistance, plante, lectine, inhibiteur de protease, Bt, revue,,RàHEtransgenose, revue, insecte, resitance, inhibiteur protease, lectine, TRANSMISSIONV Trialeurodes vaporariorum sppTRICHOPLUSIA-NICE Trypanosomes TRYPSIN-INHIBITORS PL TSETSEORE,&Ulex europaeus , UEA, lectine, insecteULTRASTRUCTURE (L URTICA-DIOICA V-ATPaseeVACUOLAR-TYPE ATPASE vegetables venomVesiculated Cellsvirus transmissioning VIRUSESTY VOLATILESwestern corn rootwormWGAoaŒ†WHEAT, EPG, comportement alimentaire, Lactuca sativa, laitue, azadirachtin, fecondite, puceron, rŽsistance, interaction plante-insecteTR#WHEAT-GERM-AGGLUTININx t*sôrJqxpNoºn&m’lxk\F?Jouanin, L. BonadŽ-Bottino, M. Girard, C. Morrot, G. Giband, M.| 1998.'Transgenic plants for insect resistance0 Plant Sci. 1311  1-11 Plant Science0 6769’‹Revue, Transgenose, Resistance, Proteine, Inhibiteur enzyme, Inhibiteur protease, Lectine, Bacillus thuringiensis, Transformation genetique  Journy, N. 1991 &Centre scolaire J.B de la Salle rapport BTS†Alectine, Acyrthosiphon pisum, puceron, $toxprot, protŽine,insecte.     voir YvanŽ]ActivitŽ biologique de quelques lectines vŽgŽtales sur le puceron du pois Acyrthosiphon pisum J TMKanost, M.R. Kawooya, J.K. Law, J.H. Ryan, R.O. van Heusden, M.C. Ziegler, R. 1991Adv. Insect Physiol.22299-396âÛRevue, $ARYL, Insecta, Proteine LSP, Hemolymphe, Stockage, Lipophorine, Lipide, Transport, Vitellogenine, Immunite, Lectine, Inhibiteur protease, Phenoloxydase, Peptide, Coagulation, Chromoproteine, Arylphorine, insecte Insect haemolymph proteins*#Kawabe, S. Fukumorita, T. Chino, M. 1980\VCollection of rice phloem sap from stylets of homopterous insects severed by YAG laserPlant Cell Physiol.i217e 1319-1327sPJHomoptera, Laser YAG, Phloeme, Stylectomie, $PHLOEM, Poaceae, Oryza sativa 489iF@Keinanen, K. Kohr, G. Seeburg, P.H. Laukkanen, M.L. Okerblom, C. 1994 BiotechnologyBio - Technology128802-806demande le 14-09-94¤žAMINO-ACID RECEPTORS; BINDING-SITES; NMDA RECEPTORS; ION FLOW; BRAIN; SUBUNIT; recepteur, binding, insecte, SOLUBILIZATION; QUISQUALATE; KAINATE; PURIFICATION¸²We have expressed glutamate-gated ion channels in Spodoptera frugiperda Sf21 insect cells using a recombinant baculovirus system. Cells infected with recombinant baculoviruses encoding the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA)-selective glutamate receptor channel subunits GluR-B and GluR-D displayed specific high-affinity [H-3]AMPA binding (apparent dissociation constant K-d of 15 nM for GluR-B and 40 nM for GluR-D) with pharmacological profiles typical of AMPA receptors. The binding reached maximal levels (B-max of 15-30 pmol per mg of membrane protein) by 3-4 days postinfection. AMPA, glutamate and kainate triggered inward currents in GluR expressing cells, indicating assembly of functional homomeric channels. Formation of heteromeric GluR-B/D channels in doubly-infected cells was evident from the diagnostic current-voltage relations of AMPA-activated whole-cell currents. For the solubilization of the receptor, nonionic detergents Triton X-100, n-octyl-D-glucoside and n-dodecylmaltoside proved most effective. Detergent-solubilized receptor preparations were stable, retained their characteristic ligand-binding properties and bound to immobilized wheat germ lectin, demonstrating the glycosylation of insect cell-expressed GluR subunits. The expression level of 300-400 mu g of receptor protein per liter of suspension culture should facilitate production of glutamate receptors for biochemical and structural studies.TMNote K Keinanen, Vtt Biotechnol & Food Res, POB 1500, SF-02044 Espoo, FinlandVOHigh-level expression of functional glutamate receptor channels in insect cells Kennedy, G.G. Oatman, E.R. 1976jdBacillus thuringiensis and pirimicarb: selective insecticides for use in pest management on broccoliJ. econ. Entomol.i696s767-772oxqLepidoptera, Brassicaceae, Lutte, Bacillus thuringiensis, Pirimicarb, Synergie, Insecticide, Homoptera, Aphididae2 1419 Knowles, B.H. Ellar, D.J. 1986 J. Cell. Sci. 83 89-101Ni 0104WðƒCharacterisation , purification, recepteur,Bacillus thuringiensis, d-endotoxin, mode d'action, insecte, WGA, lectine, SBA, bindingº + A D E &‘Characterization and partial purification of a plasma membrane receptor for Bacillus thuringiensis var kurstaki lepidopteran-specific d-endotoxini L b g o † ‡  Kobayashi, M. Ishikawa, H. 1994J. Insect. Physiol."Journal of Insect Physiology401 33-38demande le 14/04/94ª£Pea Aphid; Alata; Flight Muscle Breakdown; Protein Synthesis; Programmed Cell Death; RESOLUTION 2-DIMENSIONAL ELECTROPHORESIS; PROGRAMMED CELL-DEATH; PROTEINS; RNAR We studied the changes in protein synthesis in the indirect flight muscles of alata of the pea aphid, Acyrthosiphon pisum during their development and degeneration subsequent to the final ecdysis, and obtained the following results. (1) While overall protein synthesis in flight muscles was markedly decreased during its degeneration, several proteins were induced specifically at this period. (2) In starved insects, in which the flight muscles did not degenerate, the above proteins were not induced at the same period of time. Refeeding these insects induced the same set of proteins. (3) In vitro translation of the RNA from the flight muscles suggested that induction of at least some of these proteins is regulated at the transcriptional level. (4) Injection of antibiotics that inhibit RNA and protein synthesis into insects prevented the flight muscles from degeneration. Based on these results, we suggest that flight muscle breakdown in the alate aphid, subsequent to its migratory flight, consists in programmed cell death.VOArticle H Ishikawa, Univ Tokyo, Fac Sci, Inst Zool, Bunkyo Ku, Tokyo 113, JapantœXMechanisms of histolysis in indirect flight muscles of alate aphid (Acyrthosiphon pisum) D W òëKoziel, M.G. Beland, G.L. Bowman, C. Carozzi, N.B. Crenshaw, R. Crossland L. Dawson, J. Desai, N. Hill, M. Kadwell, S. Launis, K. Lewis, K. Maddox, D. McPherson, K. Meghji, M.R. Merlin, E. Rhodes, R. Warren, G.W. Wright, M. Evola, S.V.Ø 1993ªyField performance of elite transgenic maize plants expressing an insecticidal protein derived from Bacillus thuringiensis c Bio/Technology112@194-200Bio/TechnologyNi 1174ø³mais, rŽsistance, plante transgenique, insecte, sŽlection varietale, tests en champ, proteine insecticide, Bacillus thuringiensis, Bt, CryIA(b), CaMV 35S, biomol, biotechnologie, l „ JDKumar, M.A. Timm, D.E. Neet, K.E. Owen, W.G. Peumans, W.J. Rao, A.G. 1993¼xCharacterization of the lectin from the bulbs of Eranthis hyemalis (winter aconite) as an inhibitor of protein synthesis 1 B J. Biol. Chem. 268T33 25176-25183&Journal of Biological Chemistry  4193ZAMINO-ACID-SEQUENCE; POKEWEED ANTIVIRAL PROTEIN; A-CHAIN; PLANT-LECTINS; ABRIN-A; FLUORESCENCE; RICIN; INVITRO; LEPIDOPTERA; EXPRESSION, lectin, Eranthis hyemalis, (Winter aconite), inhibiteur de la synthese proteique, inhibitor of protein synthesis, $toxprot, lectine, insecteo ‘ £ VPArticle AG Rao, Pioneer HI Bred Int Inc, Dept Biotechnol Res, Johnston, IA 50131 ~T}ô|Ä{øzFy¨x~wºvÊuÄ2+Kyriakides, T.R. Bedoyan, J.K. Spence, K.D. 1994"Comp. Biochem. Physiol. [A]<6Comparative Biochemistry and Physiology A - Physiology 107 3ÿ529-535Ni 01406/nodulation; coagulation; lectin; concanavalin A; insect immunity; antibacterial defense; bacterial injection; Manduca sexta; immune structures; CELL-SURFACE CHANGES; LECTIN-BINDING; BIOMPHALARIA-GLABRATA; EXTATOSOMA-TIARATUM; HEMOCYTES; DROSOPHILA; HEMOLYMPH, mode d'action, binding, recepteur, mannose,VOArticle KD Spence, Washington State Univ, Dept Microbiol, Pullman, WA 99164 USAnhHemocoel distribution of concanavalin a among the tissues of manduca sexta following bacterial injection6/Lepier, A. Azuma, M. Harvey, W.R. Wieczorek, H.n 1994b[K+/H+ antiport in the tobacco hornworm midgut: the k+-transporting component of the k+ pump, J Exp Biol&Journal of Experimental Biology, ^XBidder Building, Cambridge Commercial Park, Cowley Rd, Cambridge CB4 4DL, United Kingdom Company of Biologists Ltdi 196,361-373c 0022-0949ûK+/H+ antiport; plasma membrane; V-ATPase; potassium pump; insects; Manduca sexta; midgut; MANDUCA-SEXTA MIDGUT; VACUOLAR-TYPE ATPASE; PLASMA-MEMBRANE; PROTON PUMP; V-ATPASE; INSECT EPITHELIA; ACTIVE-TRANSPORT; CONCANAVALIN-A; ION-TRANSPORT; H+-ATPASELðéThe midgut of the tobacco hornworm secretes K+ across the apical plasma membrane of its goblet cells. This secondary K+ transport results from K+/H+ antiport energized by the proton-motive force generated by a primary, H+-transporting plasma membrane V-ATPase. Thus, the lepidopteran midgut constitutes a well-established example of the emerging concept that the proton-motive force is an alternative to the classical sodium-motive force for the energization of animal plasma membranes. K+/H+ antiport in the tobacco hornworm midgut is electrophoretic, exchanging 2H(+) for 1K(+). Under physiological conditions, it is energized by the voltage component of the proton-motive force. The strong coupling of electrophoretic K+/2H(+) antiport with the electrogenic V-ATPase provides, in principle, the minimal device for the alkalization of the midgut lumen to pH values higher than 11. K+/H+ antiport is insensitive to bafilomycin A1, but is inhibited by amiloride or Concanavalin A. Lectin staining of blots after SDS-PAGE revealed several glycosylated polypeptides in the goblet cell apical membrane which are not part of the V-ATPase and thus are candidates for the antiporter protein. Current efforts are focused on the isolation of the K+/H+ antiporter.hXRArticle H Wieczorek, Univ Munich, Inst Zool, Luisenstr 14, D-80333 Munich, Germany Liener, I.E. 1986 2+Liener, I.E. ; Sharon, N. ; Goldstein, I.J.RLThe lectins: properties, functions and applications in biology and medecine.  Orlando (USA) Harcourt Brace Jovanovichn527-554& Acadamic Press Inc. (London) Ltd biblio laboïhb$toxprot, lectine, Con A, GNA, mode d'action, revue, biologie molŽculaire, reconnaissance, insecte6/Nutritional signifiance of lectins in the dietseLis, H. Sharon, N. 1986& Biological properties of lectinsRKThe lectins: properties, functions and applications in biology and medecinea  Orlando (USA)r F@Liener, I.E. ; Sharon, N. ; Goldstein, I.J., Acadamic Press Inc.266-293 biblio labo hb$toxprot, lectine, Con A, GNA, mode d'action, revue, biologie molŽculaire, reconnaissance, insecteLis, H. Sharon, N. 1986 2+Liener, I.E. ; Sharon, N. ; Goldstein, I.J.RLThe lectins: properties, functions and applications in biology and medecine.  Orlando (USA) Harcourt Brace Jovanovich­294-370& Acadamic Press Inc. (London) Ltd biblio labohb$toxprot, lectine, Con A, GNA, mode d'action, revue, biologie molŽculaire, reconnaissance, insecteApplications of lectinseJDLuo, K. Sangadala, S. Masson, L. Mazza, A. Brousseau, R. Adang, M.J. 1997§The Heliothis virescens 170kDa aminopeptidase functions as ''receptor A'' by mediating specific Bacillus thuringiensis Cry1A delta-endotoxin binding and pore formation   ` v "Insect Biochem. Molec. Biol.27 8-9 735-7430)Insect Biochemistry and Molecular Biologyà 6779`YAminopeptidase, Bacillus thuringiensis, Toxine, Recepteur, Lectine, N-acetylgalactosamineMac Gaughey, W.H. 1986HBInsect resistance to biological insecticide Bacillus thuringiensisSciencei 229c193-195t 376E\ULepidoptera, Denree stockee, Bacillus thuringiensis, RŽsistance, SŽlection, EvolutionEˆMaccutchen, B.F. Choudary, P.V. Crenshaw, R. Maddox, D.W. Kamita, S.G. Palekar, N. Volrath, S.L. Fowler, E. Hammock, B. Maeda, S.– 1991 Biotechnology9848-852º Biotechnology8 2890tmInsecticide, Lutte biologique, Virus, $TOXPROT, Neurotoxicite, Scorpionidae, Toxine, Baculovirus, Lepidoptera<tnDevelopment of a recombinant baculovirus expressing an insect-selective neurotoxin: potential for pest control("Maison, P. Kerlan, C. Massonie, G. 1984ðƒDifferences in varietal resistance to the transmission of plum pox virus by Myzus persicae Sulzer to peach Prunus persica L. Batsch K Z k y @9SŽlection pour la rŽsistance aux insectes et aux acariens  OILB/SROP 71-72 678jcHomoptera, Aphididae, Myzus persicae, Rosaceae, Arbre, RPI, RŽsistance, Specificite, Virus, VectionxJCMartinez-Ramirez, A.C. Gonzalez-Nebauer, S. Escriche, B. Real, M.D. 1994$Biochem. Biophys. Res. Commun.:3Biochemical and Biophysical Research CommunicationsW 201€2L782-787Ni 0173LB;BBMV, intestin, recepteur, mode d'action, lectine, manduca,iòëThe CryIA(a) CryIA(b) and CryIA(c) Bacillus thuringiensis insecticidal crystal proteins (ICPs) were used in ligand-blot experiments to detect specific binding proteins in brush-border membrane vesicles (BBMV) of Manduca sexta. We identified a protein which binds these three CryIA-type ICPs. The apparent molecular mass of the protein, estimated on SDS-PAGE, was 210 kDa as was the CryIA(b) binding protein previously described by Vadlamudi and col. We have also demonstrated, in ligand blot experiments, that CryIA(a) and ClyIA(c) compete with CryIA(b) for binding this 210 kDa protein. Properties of the binding molecule can be correlated with knowledge previously aquired through radiolabelled binding experiments. (C) 1994 Academic Press, Inc.…TNArticle AC Martinezramirez, Univ Valencia, Dept Genet, E-46100 Valencia, Spainê}Ligand blot identification of a Manduca sexta midgut binding protein specific to three Bacillus thuringiensis CryIA-type ICPsa   - W m  $+ÐU<8Lectine, Revue, Transgenose, Resistance, Lutte varietale 83Lectine, RŽsistance, Genetique, insecte, gŽnŽralitŽÀXXSLectine, Toxicite, Galanthus nivalis, Intestin, Mammifere, $TOXPROT, BBMV, Rat, GNA–x0-Lectine, Toxine, Induction, $toxprot, insecte LECTINeSOD>lectines, GNA, mode d'action, Hemiptera, Aphelinus abdominalis{\<6lectines, GNA, mode d'action, Hemiptera, Aphidius erviWËlglectines, GNA, mode d'action, Hemiptera, Nephotettix virescens, Nilaparvata lugens, plante transgeniqueËÀ LectinssoLens culinarisnsi LEPIDOPTERAGHôðLEPIDOPTERA, Acyrthosiphon pisum (Harris) (Homoptera:Aphididae), Aphidius ervi Haliday (Hymenoptera:Braconidae), ecdysteroide, physiologie, interaction insecte-insecte, SDS-PAGE, electrophorse, biochimie, mŽtabolisme, IsoenzymeshŽmolymphehtqLepidoptera, Brassicaceae, Lutte, Bacillus thuringiensis, Pirimicarb, Synergie, Insecticide, Homoptera, AphididaeXULepidoptera, Denree stockee, Bacillus thuringiensis, RŽsistance, SŽlection, EvolutionLEPTINOTARSA DECEMLINEATAxuLignine, Compose aromatique, Inhibiteur protease, Lectine, Glycoside, Saponine, Antibiose, Vertebrata, Revue, insectelipopolysaccharide!  LOCALIZATIONILucilia cuprinaboLUCILIA-CUPRINALFTQlutte intŽgrŽe, insectes, rŽsistance, sŽlection, gestion rŽsistance, variabilite,´®lutte intŽgrŽe, plante resistante, insecte, IPM , Integrated Pest Management, gestion rŽsistance, Nephotettix virescens, Nilaparvata lugens, riz, lutte biologique, sŽlection,0+Lymantria dispar nuclear polyhedrosis virus ¸³mais, rŽsistance, plante transgenique, insecte, sŽlection varietale, tests en champ, proteine insecticide, Bacillus thuringiensis, Bt, CryIA(b), CaMV 35S, biomol, biotechnologie,| MAIZE$!MALACOSOMA DISSTRIA , LEPIDOPTERA maladieon Manduca sextaMANDUCA-SEXTA MIDGUThdmarqueur moleculaire, plante, breeding, sŽlection, RFLP, RAPD, $biomol, $selec, insecte, rŽsistance,  MECHANISMMEDIATED UPWIND FLIGHTIPAMegoura viciaeogrMelanaspis obscura }PLMELON, parasitoide, Aphidius , test de sŽlection, mŽcanisme de la rŽsistance MEMBRANERmicro electrode midguta sMidgut Antigensbo miellatË`miellat, HOMOPTERAm milieu artificielTPmilieu artificiel, mŽtabolisme, puceron, aphide, EPG, Vicia faba, aposymbiotique$ milieu artificiel, test de choixs,&mode d'action, lectine, GNA, HemipteraWË$mode d'action, lectine, insecte 83mode d'action, lectine, insecte, Lacanobia oleraceaR#40mode d'action, revue, immunitŽ, lectine, insecte,&mode d'actionTHURINGIENSIS d-ENDOTOXINeur MOLECULAR CHARACTERIZATIONUSMOLECULAR-CLONINGMonoclonal Antibodies MonophagieicaMOSAIC VIRUS-35S PROMOTERMOSQUITO OVIPOSITIONHmultiple pest rŽsistance  MUTAGENESISSSMyzus persicaeielN-Acetylglucosamine GèåN-linked glycan, high-mannose type oligosaccharide, Con A, glycoproteine, lectine, affinodetection, immunodetection, biosynthese, maturation, fonction, interaction cellulaire, revue, $toxprot, plante, insecte, lectine, gŽnŽralitŽ nematodes$NEPHOTETTIX-VIRESCENS HOMOPTERA ,(Neurotoxicite, Scorpionidae, Venin, $nic`¨¥Nilaparvata lugens, isozyme, polymorphisme, enzyme, population, migration, isoelectic focusing (IEF), Žlectrophorse, insecticide, rŽsistance, Homoptera, Delphacidae‹Nilaparvata lugens, Nephotettix, Galanthus nivalis, Agglutinine, Ble, Lipoxygenase, Milieu artificiel, Lectine, WGA, $toxprot, GNA, insecteKNIVALIS L LECTINRNMDA RECEPTORSEPT NOCTUIDAE nodulation NUCLEAR POLYHEDROSIS-VIRUS MENUCLEOTIDE-SEQUENCE odeur olfactionolfaction, VOLATILES(ONION THRIPS THYSANOPTERAOPTICAL BRIGHTENERSS- ORIENTATIONA  OrthopteranhipmOrthoptera, Locusta migratoria, Agglutinine, Lectine, Immunite, Hemolymphe, Hemocyte, Reconnaissance, insecte Oviposition, plant-feeding, Ecologie, Insecte, Agriculture, Temperature, SŽlection, revue, prŽfŽrence, RPI, acceptation, choix, sŽlection du site alimentaireparaphyletic taxon!  PARASITISMDAE PARASITOIDeND Pathogenesis-Related Proteins Pea Aphid¶·¸¹º¹¸¸µ¹¸·¹¸·¸ºº··¸¸¸¸»¹¹¸¹¸·¶´µ¸º¸·¸¸¶¶······¶·¶´¶¶³¸¹¶µ¸¸¸¶¶¶¶·¶··µµ··¶¸¸¶µ¶······¶¶¶¶¶µ´µ¶¶µ¶··¶µ´µ´³²¶¸µ¶´³²³´³³´´´µ´´³³³´²´µµ´´µµ´µ´´´µ´²®±±¯¯±²²³±°°³µ¶´´´µ³±²³±³³±±±¯¯±²´±²³²³³²±°²³²±²°°°²²²²±²²³³³³³²´²±°°±±²¯®°²°®¯¯°°°±°±±°®¯°®®¯¯®¯¯¯¯°±°°°¯¯¯®®®¯¸¸¸¹¹¸···¹¸·¹¸·¸ºº¶¶¸º¸¹º¹¹¹¹¹·µ¶·¹¹··¹º····¶··¶µ¶·¶¸¶³·¹¶µ···¶·····¸¸·¶¸¶´µ¸·´³¸¸¸·¶·¶¶¶¶µµ´µµµ¶··¶¶´³´µµ´¸¸µµ³³´³²³´³¶µ´³²²³´´·¶¶´´´´´µµ³³´µµµ²³³±±²´³³±°°²¶·´µµµ³±²²¯²´³²±°±²³´°°³²²´³±°±±±±±°°¯±´´±°²²³³´´´³µ²²°°±±±±¯°±¯®±°°°°°°°°¯¯°±°¯¯¯­¯®­­°²°°°®®®¯¯®® ˜Í Adams1993 Adams1994 Adang1995z Adang1997Albrecht1994 Alexander1988 Altabella1990 Ando19818 Antunes1994 Applebaum1970 Applebaum1972^ Arcus1986É Ary1989v Azuma1994U Backus1993T Backus1998V Backus2000½ Bakker19941§Balasubramaniam19948Barbieri1991xœ Bardocz1990› Bardocz1993 Bardocz1996€ Bastard1984ƒ Batterham1995u Bedoyan1994s Beland1993 Bell1999xB Berberich1993 Bernays1994™Bharathi1998x  Biggs1994 Bliss1988 BonadŽ Bottino1993-ªBonadŽ Bottino1995-kBonadŽ-Bottino1998,Ç Bondari1995' Bordat19949½ Bosch1994E Boulter1983G Boulter1987  Boulter1990  Boulter1990 Boulter1990 Boulter1990J Boulter1992  Boulter1993\ Boulter1993° Boulter1994 Bournoville1980O Bournoville1994s Bowman1993 Brabant1993,Brehelin1989-Brehelin1994¦ Broekaert1993 Brousseau1995z Brousseau1997› Brown1993 Brown1994N Bryden19898 Burgess1994º Burgess1994$ But™t19951 Cadogan1994Caillaud1996x¢ Calatayud1990callahan1992x Cameron1995É Campos1989 Cardona1988 Carlini1991s Carozzi1993Carrire1995ÉCarvalho198992 Casey1994 Casida1990ˆ Causse199796 Causse1998 Chapman1994Î Charles20047Chekkafi1993n Chen1996n Chino1980 Chino1981|Choudary19919‚Choudary19911 Chrispeels1990Í Chrispeels1991Íb Chrispeels1991® Chrispeels1995 Christeller1994·Christou1999x>Christou2000x Clark2001 Coelho19944 Cohen1990 Cole1994  Couty2001 Couty2001® Craig1995|Crenshaw19919‚Crenshaw19911sCrenshaw1993xWCrenshaw1995Cronshaw1989x" Czapla1990U Czapla1993  Czapla1994! Czapla1997T Czapla1998Z Czapla19988Ê Danesh1992u davis1992# Dawson1987s Dawson19939$de Jager1995x$ de Jong1995 de la Vina2001%de Ponti1982x7Delaunay1993n¢ Delobel1990 Delobel1996s Desai1993F Dewey1984& Dhillon1991” Digilio1995G Dobie1987L Dobie1990'Dogimont19941 Donaldson1994( Dorschner1993) Dorschner1993Æ Douglas1995F Dove19844H Down1995+ Down1996  Down19999· Down19991* Down2000  Down20011, Drif1989`- Drif1994`7Driouich1993n. Edmonds1994 Edwards1990 Edwards1999< Edwards2001= Edwards2001/ Ehler19950 Eigenbrode19941Eisemann1994xq Ellar19862 Erb19943Escriche1994x~Escriche1994u4 Estada19945 Etzler1986s Evola1993œ Ewen19909› Ewen19939ˆ Fabre19976 Fabre19987 Faye1993¢ Febvay19909£ Febvay1992 « Febvay19933¬ Febvay19944¤ Febvay19955Î Febvay20044Ï Febvay20044½ Feng19944F Fenton19849N Fenton198988 Ferrari19914 Ferre19943 FerrŽ1994: Fitches1997; Fitches1998 Fitches19999 Fitches1999< Fitches2001= Fitches20017Fitchette-Laine1993KFlemming199112 Flickinger1994c Foard1978> Foissac2000* Ford2000 | Fowler19911‚ Fowler19911Í Fowler19939@ Fritz1992? Fritz1995A Fry1994B Fuchs1993n Fukumorita1980Í Fukumorita1981C Furk1993`E Gatehouse1983F Gatehouse1984D Gatehouse1986G Gatehouse1987N Gatehouse1989  Gatehouse1990  Gatehouse1990  Gatehouse1990 Gatehouse1990 Gatehouse1990 Gatehouse1990L Gatehouse1990[ Gatehouse1990K Gatehouse1991K Gatehouse1991J Gatehouse1992J Gatehouse1992\ Gatehouse1993˜ Gatehouse1993˜ Gatehouse1993¶ Gatehouse1993 Gatehouse1994° Gatehouse1994° Gatehouse1994H Gatehouse1995H Gatehouse1995M Gatehouse1995M Gatehouse1995¤ Gatehouse1995+ Gatehouse1996+ Gatehouse1996­ Gatehouse1996­ Gatehouse1996: Gatehouse1997: Gatehouse1997; Gatehouse1998I Gatehouse1998I Gatehouse1998™ Gatehouse1998™ Gatehouse1998 Gatehouse1999 Gatehouse1999· Gatehouse1999* Gatehouse2000* Gatehouse2000> Gatehouse2000> Gatehouse2000 Gatehouse2001< Gatehouse2001< Gatehouse2001< Gatehouse2001= Gatehouse2001Ï Gatehouse2004k Giband1998ik Girard1998iOGirousse1994®Gollasch199557 Gomord1993a~Gonzalez-Nebauer1994ÀÉ Grant1989œ Grant1990P Grant1991Q Grant1993› Grant1993 Grant1996< Greene20010 Greenplate1994Í Greenway1994x# Griffiths1987JDGatehouse, A.M.R. Hilder, V.A. Powel, K. Boulter, D. Gatehouse, J.A. 1992b[Potential of plant-derived genes in the genetic manipulation of crops for insect resistanceÌ6/Proc. 8th Int. Symp. Insect-Plant Relationships Dordrecht (NDL) HAS.B.J. Menken, J.H. Visser & P. Harrewijn, Ed¡ Kluwer Acad. Publ.221-234 3403ª£$nic, $TOXPROT, Lectine, Inhibiteur protease, Genie genetique, Revue, RŽsistance, Transgenose, Lepidoptera, Orthoptera, Coleoptera, Homoptera, WGA, insecte, plante4.Gatehouse, A.M.R. Hilder, V.A. Gatehouse, J.A. 1992:4Control of insect pests by plant genetic engineeringProc. r. Soc. Ser. B.eProc. r. Soc. Ser. B.J99 51-60NHTransgenose, Revue, Insecta, Inhibiteur protease, Bacillus thuringiensis‰Gatehouse, A.M.R. Shi, Y. Powell, K.S. Brough, C. Hilder, V.A. Hamilton, W.D.O. Newell, C.A. Merryweather, A. Boulter, D. Gatehouse, J.A.Œ 1993>7Approaches to insect resistance using transgenic plants "Phil. Trans. R. Soc. Lond. B 342 1301279-286ŒVOPhilosophical Transactions of the Royal Society of London Series B - Biological  428381Revue, RŽsistance, $TOXPROT, Insecta, Transgenose JIP༶Gatehouse, A.M.R. Hilder, V.A. Powell, K.S. Wang, M. Davison, G.M. Gatehouse, L.N. Down, R.E. Edmonds, H.S. Boulter, D. Newell, C.A. Merryweather, A. Hamilton, W.D.O. Gatehouse, J.A. 1994LEInsect-resistant transgenic plants: choosing the gene to do the 'job'.Biochem. Soc. Trans.& Biochemical Society Transactions224 944-949 81Revue, RŽsistance, Insecta, $TOXPROT, Transgenose2,Gatehouse, A.M.R. Down, R.E. Gatehouse ‡0†…„Bƒè‚®ö€œ 4>8Masson, L. Lun, Y.J. Mazza, A. Brousseau, R. Adang, M.J. 1995–QThe CryIA(c) receptor purified from Manduca sexta displays multiple specificities $ 1 J. Biol. Chem. .'9650 Rockville Pike, Bethesda, MD 20814 2+Amer Soc Biochemistry Molecular Biology Inc 27035 20309-20315ÿ&Journal of Biological Chemistry 0021-9258ðéBRUSH-BORDER MEMBRANE; THURINGIENSIS DELTA-ENDOTOXINS; SURFACE-PLASMON RESONANCE; BUTTERFLY PIERIS-BRASSICAE; PLANAR LIPID BILAYERS; BACILLUS-THURINGIENSIS; SELECTIVE CHANNELS; BINDING-SITES; BOMBYX-MORI; PROTEINS, recepteur, Bt, BBMThe kinetic binding characteristics of four Bacillus thuringiensis CryI insecticidal crystal proteins to a Cry-binding protein, purified from Manduca sexta brush-border vesicles, were analyzed by an optical biosensor. This 120-kilodalton binding protein, previously determined to be aminopeptidase N, was converted to a 115-kilodalton water-soluble form by removing the attached glycosylphosphatidylinositol anchor with phospholipase C. The solubilized form recognized the three major subclasses of CryIA toxins but not CryIC even though all four CryI proteins are toxic to larvae of M. sexta. CryIA(a) and CryIA(b) toxins bound to a single site on the solubilized aminopeptidase N molecule whereas CryIA(c) bound to two distinct sites. Apparent kinetic rate constants were determined for each binding reaction. All three CryIA toxins exhibited moderately fast on rates (similar to 10(-5) M(-1) s(-1)) and a slow reversible off rate (similar to 10(-3) s(-1)). Although the second CryIA(c)-binding site retained a moderately fast association rate, it was characterized by a rate of dissociation from the aminopeptidase an order of magnitude faster than observed for the other CryIA-binding sites. CryIA(c) binding to both sites was strongly inhibited in the presence of N-acetylgalactosamine (IC50 = 5 mM) but not N-acetylglucosamine, mannose, or glucose. CryIA(a) and CryIA(b) binding were unaffected in the presence of the same sugars. Our results serve to illustrate both the complexity and the diverse nature of toxin interactions with Cry-binding proteins.xqArticle L Masson, Natl Res Council Canada, Biotechnol Res Inst, 6100 Royalmount Ave, Montreal, Pq H4P 2R2, Canadaq4-Massonie, G. Monet, R. Bastard, Y. Maison, P. 1984¨cHeritability in peach of the hypersensitive reaction to the green peach aphid Myzus persicae Sulzer N \ @9SŽlection pour la rŽsistance aux insectes et aux acariens  OILB/SROPÿ69 677 RLHomoptera, Aphididae, Myzus persicae, Rosaceae, Arbre, RPI, Hypersensibilite McCall, P.J. Cameron, M.M. 1995.(Oviposition pheromones in insect vectorsParasitol. Today d^Elsevier Science Ltd, The Boulevard, Langford Lane,, Kidlington, Oxford, Oxon, England OX5 1GB Elsevier Sci Publ Ltd119l352-355Parasitology Today 0169-4758Ni 0639d¶¯SANDFLY LUTZOMYIA LONGIPALPIS; MEDIATED UPWIND FLIGHT; MOSQUITO OVIPOSITION; SYNTHETIC ATTRACTANT; DIPTERA; PSYCHODIDAE; CULICIDAE; BEHAVIOR; TSETSE; SITE, pheromone, insecte,gleOviposition aggregation pheromones occur in a range of insect groups including Diptera, where they mediate oviposition in four different families of disease vectors. In this paper, Philip McCall and Mary Cameron discuss the selection pressures favouring oviposition pheromones and speculate on their potential applications in disease monitoring and control.,‰Article PJ Mccall, Univ Liverpool, Liverpool Sch Trop Med, Div Parasite & Vector Biol, Pembroke Pl, Liverpool L3 5QA, Merseyside, England†€McCutchen, B.F. Choudary, P.V. Crenshaw, R. Maddox, D.W. Kamita, S.G. Palekar, N. Volrath, S.L. Fowler, E. Hammock, B. Maeda, S. 1991tnDevelopment of a recombinant baculovirus expressing an insect-selective neurotoxin: potential for pest control Biotechnology 9848-852 2890tmInsecticide, Lutte biologique, Virus, $TOXPROT, Neurotoxicite, Scorpionidae, Toxine, Baculovirus, Lepidoptera"Mckenzie, J.A. Batterham, P. 1995$Insecticide resistance - replyTrend Ecol. Evolut. f_Elsevier Science Ltd, The Boulevard, Langford Lane,, Kidlington, Oxford, United Kingdom OX5 1GBo Elsevier Sci Publ LtdX104 165$Trends in Ecology & Evolution  0169-5347 TNLetter JA Mckenzie, Univ Melbourne, Dept Genet, Parkville, Vic 3052, AustraliaXQETHYL METHANESULFONATE MUTAGENESIS; LUCILIA-CUPRINA; SƒLECTION; GENETICS; DIPTERAaMeeusen, R.L. Warren, G. 1989Annu. Rev. Entomol.34373-381 248460Insect control with genetically engineered crops¨xRevue, RŽsistance, Insecte, Transgenose, Lutte varietale, Inhibiteur protease, $TOXPROT, Bacillus thuringiensis, lectine Y  Milner, R.J. 1994Agr. Ecosyst. Environ.*$Agriculture Ecosystems & Environment491 9-13demande le 14/09/94 CEREUS¶¯Bacillus thuringiensis (Bt) was isolated from a flour moth collected in the German province of Thuringia and described by Berliner in 1915. The same organism had already been described by Ishiwata in 1902 as Bacillus sotto from Japan where it causes a wilt disease of silkworm caterpillars, but the description was not known to Berliner. Bt is now the accepted name for a range of aerobic spore-forming bacteria which form an insect toxic crystal during sporulation. However, many bacteriologists consider Bt to be a variant of Bacillus cereus, a ubiquitous soil-inhabiting bacterium. Since the pioneering work of Steinhaus in California in the early 1950s, there has been considerable commercial interest and products are now sold in most countries of the world for control of caterpillars (var. kurstaki, entomocidus, galleriae and aizawai), mosquito and blackfly larvae (var. israelensis) and beetle larvae (var. tenebrionis and san diego).XRArticle RJ Milner, CSIRO, Div Geophys, Gpb Box 1700, Canberra, Act 2601, Australiaf!History of Bacillus thuringiensisC   !  Milner, R.J. 1994Agr. Ecosyst. Environ.*$Agriculture Ecosystems & Environment491 9-13demande le 14/09/94 CEREUS¶¯Bacillus thuringiensis (Bt) was isolated from a flour moth collected in the German province of Thuringia and described by Berliner in 1915. The same organism had already been described by Ishiwata in 1902 as Bacillus sotto from Japan where it causes a wilt disease of silkworm caterpillars, but the description was not known to Berliner. Bt is now the accepted name for a range of aerobic spore-forming bacteria which form an insect toxic crystal during sporulation. However, many bacteriologists consider Bt to be a variant of Bacillus cereus, a ubiquitous soil-inhabiting bacterium. Since the pioneering work of Steinhaus in California in the early 1950s, there has been considerable commercial interest and products are now sold in most countries of the world for control of caterpillars (var. kurstaki, entomocidus, galleriae and aizawai), mosquito and blackfly larvae (var. israelensis) and beetle larvae (var. tenebrionis and san diego).XRArticle RJ Milner, CSIRO, Div Geophys, Gpb Box 1700, Canberra, Act 2601, Australiaf!History of Bacillus thuringiensisC   !  Monties, B.ÿ 1981 COSTES C. (Ed.)*#Proteines foliaires et alimentation $Gauthiers-Villars, Paris (FRA) 94-120 905|uLignine, Compose aromatique, Inhibiteur protease, Lectine, Glycoside, Saponine, Antibiose, Vertebrata, Revue, insecteâLes antinutritionnelsâ ’V‘ªÆ`ŽÄŒŽ‹*Š T‰„ˆLEMourey, L. Pedelacq, J.D. Fabre, C. Causse, H. RougŽ, P. Samama, J.P.¢ 1997ЋSmall-angle x-ray scattering and crystallographic studies of arcelin-1: An insecticidal lectin-like glycoprotein from Phaseolus vulgaris L. v ˆ "Prot. Struct. Func. and Gen.294433-442›2+PROTEINS: Structure, Function, and Genetics 6685\UArcelin, Cristallisation, Lectine, Phaseolus vulgaris, Glycoproteine, Spectroscopie XàHAMurdock, L.L. Huesing, J.E. Nielsen, S.S. Pratt, R.C. Shade, R.E. 1990Phytochemistry291 85-89Phytochemistry 2701 importŽ de 4Dh>8Biological effects of plant lectins on the Cowpea Weevil‰Lectine, Callosobruchus maculatus, Antibiose, Activite biologique, RŽsistance, Transformation genetique, $toxprot, mode d'action, insectel<6Narvaez-Vasquez, J. Orozco-Cardenas, M.L. Ryan, C.A. 1992”Differential expression of a chimeric CaMV-tomato proteinase Inhibitor I gene in leaves of transformed nightshade, tobacco and alfalfa plantsPlant. Mol. Biol.Plant Molecular Biology20 1149-1157 3583ÈÂProteinase Inhibitor Genes; Camv-35S Promoter; Transgenic Plants; MOSAIC VIRUS-35S PROMOTER; MECHANISM; DEFENSE; COMPONENTS; INSECTS, Nicotiana tabacum, Medicago sativa, Solanum nigrum, $toxprotThe open reading frame and terminator region of a wound-inducible tomato Inhibitor I gene, regulated by the CaMV 35S promoter, was stably integrated into the genomes of nightshade (Solanum nigrum), tobacco (Nicotiana tabacum), and alfalfa (Medicago sativa), using an Agrobacterium-mediated transformation system. The expression of the foreign Inhibitor I gene in leaves of each species was studied at the mRNA and protein levels. The levels of Inhibitor I protein present in leaves of each species correlated with the levels of mRNA. The average levels of both mRNA and Inhibitor I protein were highest in leaves of transgenic nightshade plants (over 125 mug of Inhibitor I per g tissue), less in tobacco plants (about 75 mug/g tissue), and lowest in leaves of transgenic alfalfa plants (below 20 mug/g tissue). Inhibitor I protein was observed in all tissues throughout transgenic plant species, but inhibitor concentration per gram of tissue was 2-3 times higher in young developing leaf tissues and floral organs. The differences in the expression of the CaMV-tomato Inhibitor I gene among the different plant genera suggests that either the rate of transcription of the foreign gene or the rate of degradation of the nascent Inhibitor I mRNA varies among genera. Using electron microscopy techniques, the newly synthesized pre-pro-Inhibitor I protein was shown to be correctly processed and stored as a mature Inhibitor I protein within the central vacuoles of leaves of transgenic nightshade and alfalfa. The results of these experiments suggest that maximal expression of foreign proteinase inhibitor genes, and perhaps other foreign defense genes, may require gene constructs that are fashioned with promoters and terminators that allow maximum expression in the selected plant species.ŽPIArticle CA Ryan, Washington State Univ, Inst Biol Chem, Pullman, WA 99164ø Natori, S. 1990LEDual Functions of Insect Immunity Proteins in Defence and Development Res. Immunol. 141938-939 2772Œ…Insecta, Immunite, Revue, Developpement, Defense, Lectine, Reconnaissance cellulaire, Galactose, Expression stade specifique, insecteV Natori, S. 19944-Function of antimicrobial proteins in insectsd Marsh, J. Goode, J.A.Antimicrobial Peptides 81Baffins Lane, Chichester, United Kingdom PO19 7UD John Wiley & Sons Ltd 186123-132Ciba Foundation Symposia 0-471-95025-4Ni 0591ÎÈlectine, immunitŽ, insecte, PEREGRINA FLESH-FLY; SARCOPHAGA LECTIN GENE; ANTIBACTERIAL PROTEINS; HYALOPHORA CECROPIA; SARCOTOXIN-I; BACTERICIDAL PROTEIN; PURIFICATION; HEMOLYMPHe, Sarcophaga peregrina82We have isolated and characterized various antimicrobial proteins from the haemolymph of Sarcophaga peregrina (flesh fly) larvae. Of these the sarcotoxin I family is a group of proteins mainly active against Gram-negative bacteria whereas sapecin is active mainly against Gram-positive bacteria. In addition to its function in defence, sapecin also plays a role in insect development. Recently, we identified a hendecapeptide of the sapecin homologue sapecin B that has the same antibacterial activity as the original sapecin B. Both sarcotoxin I and sapecin are inducible proteins synthesized de novo by the fat body and/or haemocytes and secreted into the haemolymph when the insect is in the acute phase response to bacterial infection. Antifungal protein (AFP) is constitutively present in the haemolymph and is active against certain fungi but not bacteria. These various antimicrobial proteins interact with microbial membranes. Sarcotoxin I interferes with membrane functions such as ATP synthesis and amino acid transport. The fungicidal activity of AFP is enhanced synergistically by sarcotoxin I, although sarcotoxin I alone has no appreciable antifungal activity. It is clear that the flesh fly has the ability to mount a potent defence response against microbial parasites by mobilizing several antimicrobial proteins.TMArticle S Natori, Univ Tokyo, Fac Pharmaceut Sci, Bunkyo Ku, Tokyo 113, JapanY Newby, R.C.ì 19800)The use of insects for sampling xylem sap  Ann. Bot.i45213-215aF@Stylectomie, Revue, Homoptera, Xyleme, $PHLOEM, Calcium, Miellat 2340 Ollivier, L. 1981("ElŽments de gŽnŽtique quantitative  Ollivier, L. Parisd  INRA & MassonNi 1131Labo INSA-Lyon #B75'~wgŽnŽtique quantitative, equilibre Hardy-Weinberg, insecte, population, revue, concept, sŽlection, adaptation, evolution'D>Osborn, T.C. Alexander, D.C. Sun, S.S. Cardona, C. Bliss, F.A. 1988Science 240207-210 1948HAInsecticidal activity and lectin homology of arcelin seed proteine˜’Toxicite, Lectine, Insecticide, Fabaceae, Phaseolus vulgaris, Coleoptera, Bruchidae, RPI, Defense, $TOXPROT, insecte, arceline, rŽsistance, plantePapp, M. 1990˜Yield reduction effect of cereal leaf beetle (Oulema melanopus L.) and bird cherry-oat aphid (Rhopalosiphum padi L.) on different winter wheat genotypes . > ^ p  I. Panayotov S. PavlovaBPlant lectins - Chemistry and pharmacology of natural products Cambridge (GBR) Cambridge University Press 253 Ni 1164B,&lectine, Con A, GNA, $toxprot, insectenhPusztai, A. Ewen, S.W.B. Grant, G. Brown, D.S. Stewart, J.C. Peumans, W.J. Van Damme, E.J.M. Bardocz, S. 1993 Br. J. Nutr.701313-321"British Journal of Nutrition 4089PIArticle A Pusztai, Rowett Res Inst, Bucksburn AB2 9SB, Aberdeen, Scotland"d]Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins"ÔÍAntinutritif; Insecte, RŽsistance; COWPEA WEEVIL; $toxprot, mode d'action, intestin , rat, Triticum aestivum (WGA), thorn apple (Datura stramonium), nettle (Urtica dioica), mode d'action, binding, lectine,"voPusztai, A. Koninkx, J. Hendriks, H. Kok, W. Hulscher, S. van Damme, E.J.M. Peumans, W.J. Grant, G. Bardocz, S.£ 1996ЋEffect of the insecticidal Galanthus nivalis agglutinin on metabolism and the activities of brush border enzymes in the rat small intestineP  , Nutr. Biochem.7 12677-682€Nutritional Biochemistry 6084ZSLectine, Toxicite, Galanthus nivalis, Intestin, Mammifere, $TOXPROT, BBMV, Rat, GNA R&I  19944-Des insecticides synthŽtisŽes par des plantesRecherche & Industrie 1348 09/95Ni 0306 4.sauvion, rahbŽ, transgenese, lectine, puceron,Raes, H. Verbeke, M. 1994 Tissue Cell262­223-230® Tissue & CelltNi 0109:˜’Midgut; Gut Endocrine Cells; Granulated Cells; Vesiculated Cells; Insect; Apis Mellifera (L); ULTRASTRUCTURE; IMMUNOREACTIVITY; INSECTe, intestin,^XArticle H Raes, State Univ Ghent, Zoophysiol Lab, Ledeganckstr 35, B-9000 Ghent, BelgiumÆ‚Light and electron microscopical study of two types of endocrines cell in the midgut of the adult worker honeybee (Apis mellifera) s   +$,! INVIVOCEL ION FLOWE ION-TRANSPORTIsoelectrofocusing } ISOLECTINSONsK+/H+ antiport! KAINATELA kairomonesten LASIOCAMPIDAE Lectin }HClectin, insecte, PHA, Phaseolus vulgarus, Callosobruchus maculatus,LECTIN-BINDINGHAN LectineniDAlectine, Acyrthosiphon pisum, puceron, $toxprot, protŽine,insecte<8Lectine, Bacillus thuringiensis, Revue, ***SciArtPriCommŒ‰Lectine, Callosobruchus maculatus, Antibiose, Activite biologique, RŽsistance, Transformation genetique, $toxprot, mode d'action, insecte,&lectine, Con A, GNA, $toxprot, insecteWË€´°lectine, Concanavalin A, EPG, actography, Homoptera, Aphididae, midgut, plante transgŽnique, tube digestif, mŽtabolisme, pea aphid, Acyrthosiphon pisum, binding, mode d'action,°¬lectine, Concanavalin A, physiologie, Homoptera, Aphididae, midgut, plante transgŽnique, tube digestif, mŽtabolisme, pea aphid, Acyrthosiphon pisum, binding, mode d'action,„€Lectine, Galanthus nivalis, Amaryllidaceae, Lepidoptera, Transgenose, Lacanobia oleracea, Solanaceae, Resistance, $TOXPROT, $TRG<8lectine, hemiptera, Sitobion avenae, plante transgŽnique°4/lectine, immunitŽ, insecte, PEREGRINA FLESH-FLY5°ÌÇlectine, insecte, binding, mode d'action, plante, intestin, midgut, facteur de croissance, Phaseolus vulgaris (PHA), Glycine max (SBL), Sambucus nigra (SNA), Galanthus nivalis (GNA), Vicia faba (VFL)Ì hclectine, insecte, inhibiteur protease, immunomarquage, mode d'action, recepteur, immunolocalisation| 0-lectine, insecte, legume, plante, rŽsistance,,(lectine, insecte, puceron, mode d'action€HDlectine, Lucilia cuprina:, mode d'action, $toxprot,insecte, FITC, ME lectine, mode d'action, GNA”ô$lectine, mode d'action, insecteÔ ,&lectine, mode d'action, PHA, Hemiptera€}lectine, Phaseolus vulgaris, $toxprot, Callosobruchus maculatus, Vigna unguiculata, trypsin inhibitor, insecte, mode d'action`Zlectine, plante, rŽsistance, legumineuse, inhibiteur protease, defense, insecte, predateurKpmLectine, Revue, Transgenose, Lutte varietale, Bacillus thuringiensis, Insecta, RPI, Mannose, ***SciSynPerssCLbehavior of Myzus persicae (Homoptera, aphididae) by selected compoundsR # 2 <5Myzus persicae; Electronic Monitoring System; Feeding Behavior Modification; SCHIZAPHIS-GRAMINUM; PROBING BEHAVIOR; RESISTANT; DELTAMETHRIN; TRANSMISSION; FECUNDITY; VIRUSES; WHEAT, EPG, comportement alimentaire, Lactuca sativa, laitue, azadirachtin, fecondite, puceron, rŽsistance, interaction plante-insecte& Sauvion, N. Febvay, G. RahbŽ, Y. 1993ðéMŽcanismes de la toxicitŽ de certaines lectines vŽgŽtales pour les pucerons (Homoptera : Aphididae). Potentiel d'utilisation de ces toxines protŽiques pour la crŽation de plantes transgŽniques rŽsistantes aux homoptres phloŽmophagesd0*11me Colloque de Physiologie de l'Insecte Tours - 16-17/09/1993l.(lectine, insecte, puceron, mode d'action& Sauvion, N. Febvay, G. RahbŽ, Y. 1994ØÒMŽcanismes de la toxicitŽ de certaines lectines vŽgŽtales pour les pucerons - Potentiel d'utilisation de ces toxines protŽiques pour la crŽation de plantes transgŽniques rŽsistantes aux homoptres phloŽmophages0)4emes JournŽes Interaction Plante-Insecte Rennes - 4-5/07/1994$lectine, insecte¦:4Sauvion, N. BonadŽ Bottino, M. Jouanin, L. RahbŽ, Y. 199582Les plantes transgŽniques rŽsistantes aux insectesInfoZood10 3-13Ni 0219d^transgenose, insecte, puceron, rŽsistance, plante, lectine, inhibiteur de protease, Bt, revue,ZSSauvion, N. RahbŽ, Y. Peumans, W.J. van Damme, E. Gatehouse, J.A. Gatehouse, A.M.R.ª 1996¦vEffects of GNA and other mannose binding lectins on development and fecundity of the potato-peach aphid Myzus persicae h Entomol. exp. appl.d79285-293 .'Entomologia Experimentalis et Applicata›Ni 0269¤ž$lectin, mode d'action, mannose, inhibition de croissance, Myzus persicae, insecte, binding, milieu artificial, toxicite, modelisation, rm, NPA, GNA, ASA, RSA JIP ¶(µ´À³h²t±ö°¼¯H®Ø|uSchroeder, H.E. Gollasch, S. Moore, A. Tabe, L.M. Craig, S. Hardie, D.C. Chrispeels, M.J. Spencer, D. Higgins, T.J.V. 1995 uBean a-amylase inhibitor confers resistance to the pea weevil (Bruchus pisorum) in transgenic peas (Pisum sativum L.)   ? N d q Plant Physiol. .'15501 Monona Drive, Rockville, MD 20855 "Amer Soc Plant Physiologists 1074 1233-1239Plant Physiology 0032-0889Ni 0617 HABruchid larvae cause major losses of grain legume crops throughout the world. Some bruchid species, such as the cowpea weevil and the azuki bean weevil, are pests that damage stored seeds. Others, such as the pea weevil (Brochus pisorum), attack the crop growing in the field. We transferred the cDNA encoding the alpha-amylase inhibitor (alpha-AI) found in the seeds of the common bean (Phaseolus vulgaris) into pea (Pisum sativum) using Agrobacterium-mediated transformation. Expression was driven by the promoter of phytohemagglutinin, another bean seed protein. The alpha-amylase inhibitor gene was stably expressed in the transgenic pea seeds at least to the T-5 seed generation, and alpha-AI accumulated in the seeds up to 3% of soluble protein. This level is somewhat higher than that normally found in beans, which contain 1 to 2% alpha-AI. In the T-5 seed generation the development of pea weevil larvae was blocked at an early stage. Seed damage was minimal and seed yield was not significantly reduced in the transgenic plants. These results confirm the feasibility of protecting other grain legumes such as lentils, mungbean, groundnuts, and chickpeas against a variety of bruchids using the same approach. Although alpha-AI also inhibits human alpha-amylase, cooked peas should not have a negative impact on human energy metabolism.\VArticle TJV Higgins, CSIRO, Div Plant Ind, GPO Box 1600, Canberra, Act 2601, AustraliaèâPHASEOLUS VULGARIS L; ARCELINe ; TOBACCO; EXPRESSION; LECTINeS; GENE, plante transgenique, insecte, bruche , rŽsistance , plante, transgenese, Brochus pisorum, Pisum sativum, Phaseolus vulgaris, inhibiteur protease, promoteur, Shewry, P. 1991 Oxford University PressB;1991 Annual Meeting of the Society for Experimental Biology42 238 4112B7Sutherland, P.W. Burgess, E.P.J. Main, C.A. McManus, M. 1994 non publiŽNi 0116jclectine, insecte, inhibiteur protease, immunomarquage, mode d'action, recepteur, immunolocalisation®jImmunolocalization of Potato Protease Inhibitor II in the midgut of the Black Field, Teleogryllus commodus U j Tabashnik, B.E.› 1995Insecticide resistanceTrend Ecol. Evolut.›  Ed¡ Elsevier104164-165$Trends in Ecology & Evolution  0169-5347 Ni 0641²¬POTATO BEETLE COLEOPTERA; LUCILIA CUPRINA; ARMIGERA LEPIDOPTERA; SELECTIVE MORTALITY; TOBACCO BUDWORM; GENETIC-BASIS; FIELD; NOCTUIDAE; CHRYSOMELIDAE; POPULATIONS, $lutchim\VLetter BE Tabashnik, Univ Hawaii, Dept Entomol, 3050 Maile Way, Honolulu, HI 96822 USATjallingii, W.F. 1987Insects-Plantsd]Stylet penetration activities by aphids : new correlations with electrical penetration graphsy301-306g .'LABEYRIE V.,FABRES G.,LACHAISE D. (Eds)d W. Junk Publishers2,Homoptera, Aphididae, EPG, Piqure, Ingestion 1233jcvan der Salm, T. Bosch, D. Honee, G. Feng, L.X. Munsterman, E. Bakker, P. Stiekema, W.J. Visser, B. 1994ÒŽInsect resistance of transgenic plants that express modified Bacillus thuringiensis CRYlA(b) and CRYlC genes: a resistance management strategy = S Plant Mol. Biol.261 51-59Plant Molecular BiologyBacillus thuringiensis; crystal protein; plant; Heliothis virescens; rŽsistance management; Spodoptera exigua; BRUSH-BORDER MEMBRANE; CRYSTAL PROTEIN GENES; RNA TRANSCRIPTS; TOMATO PLANTS; SEQUENCE; INVIVO; DETERMINANTS; SPECIFICITY; MUTAGENESIS; PROTOPLASTSpiTobacco and tomato plants were generated exhibiting insect resistance due to the introduction of modified cryIA(b) and cryIC genes of Bacillus thuringiensis. Limited modifications at selected regions of the coding sequences of both genes are sufficient to obtain resistance against Spodoptera exigua, Heliothis virescens and Manduca sexta. The criteria used to modify both genes demonstrate that the removal of sequence motifs potentially resulting in premature polyadenylation and transcript instability causes increased insect resistance. The expression of a cryIC-cryIA(b) fusion resulting in protection against S. exigua, H. virescens and M. sexta demonstrates the potential of expressing translational fusions, not only to broaden the insect resistance of transgenic plants, but also to simultaneously employ different gene classes in resistance management strategies.AvoArticle D Bosch, Dlo, Ctr Plant Breeding & Reprod Res, Dept Molec Biol, POB 16, 6700 AA Wageningen, NetherlandsS Visser, J.H. Piron, P.G.M. 1995šjOlfactory antennal responses to plant volatiles in apterous virginoparae of the vetch aphid Megoura viciae \  B;Spuiboulevard 50, PO Box 17, 3300 AA Dordrecht, Netherlands Kluwer Academic Publ771  37-46 0013-8703Ni 0482db\Article JH Visser, Res Inst Plant Protect Ipo Dlo, POB 9060, 6700 Gw Wageningen, NetherlandspjAphididae; attractants; electro-antennographie (EAG); kairomones; Megoura viciae; odeur; olfaction; plant volatiles; repellents; semiochimique; rŽsistance, plante, insecte, COLORADO BEETLE; LEPTINOTARSA DECEMLINEATA; HOMOPTERA; INSECTS; ORIENTATION; POTATO,( E)-2-hexenal, (E)-2-heptenal, 1-octenol-3, hexyl acetate, (Z)-3-hexenyl acetate, hexanol-1,hexanal, 2-heptanone, 3-octanone, 4-methoxybenzaldehyde (p-anisaldehyde), hexanonitrile, heptanonitrile, 1,6-hexanedithiol, butyl isothiocyanate, 4-pentenyl isothiocyanate, (-)-(1S)-beta-pinene, (+)-(S)-carvone, (-)-(R)-carvone, alpha-terpineol, linalool, citronellal.'Entomologia experimentalis et applicatalEntomol. exp. appl.eVisser, J.H. Yan, F.S. 1995”Electroantennogram responses of the grain aphids Sitobion avenae (F.) and Metopolophium dirhodum (Walk.) (Hom., Aphididae) to plant odour components 1 @ J ` J. Appl. Entomol. 0*Kurfurstendamm 57, D-10707 Berlin, Germany *#Blackwell Wissenschafts Verlag GmbH 1198 539-542$Journal of Applied Entomology 0931-2048Ni 1001 d÷HOST PLANT; LEPTINOTARSA DECEMLINEATA; COLORADO BEETLE; VOLATILES; HOMOPTERA; INSECTS; resistance, plante, Homoptera, Aphididae, comportement, electroantennographie, EAG, allŽlochimique, RPI, Sitobion avenae (F.), Metopolophium dirhodum (Walk.), Â Ð Ø î d^Article JH Visser, Dlo, Ipo, Plant Protect Res Inst, POB 9060, 6700 Gw Wageningen, NetherlandsÅ$ÄàÃhÂöÁ ÀÞVolkov, A.G. Haack, R.A. 1995@:Insect-induced bioelectrochemical signals in potato plantsBioelectrochem Bioenerg. .(PO Box 564, 1001 Lausanne 1, Switzerland "Elsevier Science SA Lausanne371L 55-60,%Bioelectrochemistry and Bioenergetics 0302-4598ÿb\chemical injury; potato beetle; induced action potential; ACTION-POTENTIALS; RESPONSES; HEATîèAction potentials and resting potentials were measured in potato plants (Solanum tuberosum L.) under different physiological conditions. External stimuli (e.g. changing temperature, wounding or exposing plant leaves or soil to certain chemical compounds) cause an action potential to be generated and change the resting potential from the original steady state level. The amplitude, polarity and the speed of action potential propagation depend on the type of external stimuli or stress. The kinetics and amplitude of the resting potential also change depending on the nature of the external stimuli. For example, in the presence of leaf-feeding larvae of the Colorado potato beetle (Leptinotarsa decemlineata (Say); Coleoptera: Chrysomelidae), the speed at which insect-induced action potentials moved downward through the stem was about 0.05 cm s(-1). The action potentials propagated downwards from the damaged leaf along the stem. When the upper leaves of potato plants were sprayed with 0.3 mi of 1 mM aqueous solution of pentachlorophenol, the effect was almost identical to that induced by Colorado potato beetle. To our knowledge, this is the first demonstration of action potential generation in plants induced by insect damage or chemical injury.^WArticle AG Volkov, Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USAü"Vondohlen, C.D. Moran, N.A. 1995@:Molecular phylogeny of the homoptera: a paraphyletic taxon J. Mol. Evol.ÿ (!175 Fifth Ave, New York, NY 10010 Springer Verlag,412<211-223$Journal of Molecular Evolution 0022-2844äÞHomoptera; Heteroptera; Hemiptera; paraphyletic taxon; phylogeny, 18S rDNA; RIBOSOMAL-RNA GENES; SECONDARY STRUCTURE; NUCLEOTIDE-SEQUENCE; EVOLUTIONARY TREES; DNA; BIOLOGY; APHID; HETEROPTERA; DIVERSITY, aphide, phylogenieÀ¹Homoptera and Heteroptera comprise a large insect assemblage, the Hemiptera. Many of the plant sap-sucking Homoptera possess unusual and complex life histories and depend on maternally inherited, intracellular bacteria to supplement their nutritionally deficient diets. Presumably in connection with their diet and lifestyles, the morphology of many Homoptera has become greatly reduced, leading to major controversies regarding the phylogenetic affiliations of homopteran superfamilies. The most fundamental question concerns whether the Homoptera as a whole are monophyletic. Recent studies based on morphology have argued that the Homoptera Sternorrhyncha (Aphidoidea, Coccoidea, Psylloidea, Aleyrodoidea) is a sister group to a group comprising the Homoptera Auchenorrhyncha (Fulgoroidea, Cicadoidea, Cercopoidea, Cicadelloidea) and the Heteroptera, making the Homoptera paraphyletic. We sequenced the 5' 580-680 base pairs of small-subunit (18S) ribosomal DNA from a selection of Homoptera, Hemiptera, and their putative outgroups, the Thysanoptera and Psocoptera, to apply molecular characters to the problem of Homoptera phylogeny. Parsimony, distance, maximum-likelihood, and bootstrap methods were used to construct trees from sequence data and assess support for the topologies produced. Molecular data corroborate current views of relationships within the Sternorrhyncha and Auchenorrhyncha based on morphology and strongly support the hypothesis of homopteran paraphyly as stated above. In addition, it was found that Homoptera Sternorrhyncha have extra, GC-rich sequence concentrated in a variable region of the 18S rDNA, which indicates that some unique evolutionary processes are occurring in this lineage.lf_Article CD Vondohlen, Idaho State Univ, Dept Biol Sci, Campus Box 8007, Pocatello, ID 83201 USA Wallace, B.d 1974 GŽnŽtique des populations  Wallace, B.È Paris MassonNi 1129labo INSA-Lyon #B56df_genetique des population, sŽlection, population, evolution, adaptation, revue, concept, insectedWang, N. Nobel, P.S. 1995ʆPhloem exudate collected via scale insect stylets for the CAM species Opuntia ficus-indica under current and doubled CO2 conentrations F Z  Ann. Bot.75525-532Annals of BotanyNi 0619.'Phloem, EDTA, stylectomie, CAM plantes,"Wayadande, A.C. Nault, L.R. 1996\VLeafhoppers on leaves: an analysis of feeding behavior using conditional probabilitiesJ. Insect Behav. (!233 Spring St, New York, NY 10013 Plenum Publ Corp91 3-22 Journal of Insect Behavior 0892-7553demandŽ le 29 mai 962+feeding behavior; electronic monitoring; virus transmission; Graminella nigrifrons; G-oquaka; Amblysellus grex; Dalbulus maidis; CHLOROTIC DWARF VIRUS; NEPHOTETTIX-VIRESCENS HOMOPTERA; PROBING BEHAVIOR; POTATO LEAFHOPPER; RICE VARIETIES; PLANT-VIRUSES; CICADELLIDAE; MAIZE; TRANSMISSION; LEPIDOPTERAleArticle LR Nault, Oklahoma State Univ, Dept Plant Pathol, 110 Noble Res Ctr, Stillwater, OK 74078 USA¬.(Welburn, S.C. Maudlin, I. Molyneux, D.H. 1994Med. Vet. Entomol.81 81-87(!Medical and Veterinary Entomology 4432ÖÏTsetse; Trypanosomes; Lectins; HEMOLYMPHE; FLY; GUT, intestin, Trypanosoma congolense, Glossina palpalis palpalis, Trypanosoma brucei rhodesiense, Glossina pallidipes, midgut, insecte, mode d'action, bindingeb[Article SC Welburn, Univ Bristol, Tsetse Res Lab, Langford House, Bristol BS18 7DU, EnglandoLFMidgut lectin activity and sugar specificity in teneral and fed tsetseÍh̸Ë,ʸÈÌÉzÇpÆ Ô$Wilkinson, T.L. Douglas, A.E. 1995¼xAphid feeding, as influenced by disruption of the symbiotic bacteria: an analysis of the pea aphid (Acyrthosiphon pisum) d w J. Insect Physiol. HAThe Boulevard, Langford Lane, Kidlington, Oxford, England OX5 1GB $Pergamon-Elsevier Science Ltd418d635-640"Journal of Insect Physiology 0022-1910dNi 0583 Pea aphids (Acyrthosiphon pisum) whose symbiotic bacteria were disrupted with the antibiotic chlortetracycline over the first 5 days after birth (i.e, aposymbiotic aphids), were able to feed from the host plant Vicia faba, as indicated by the regular production of honeydew droplets and by electrical penetration graph (EPG) recordings of stylet penetration through the plant tissues to the sieve elements, No difference was identified in the time taken by adult symbiotic and aposymbiotic aphids [24 +/- 2.4 and 24 +/- 3.0 min (mean +/- SE), respectively] to penetrate the plant tissues and puncture the sieve elements during the probes which resulted in sustained phloem feeding, 7/8-day-old aposymbiotic larvae produced less honeydew (0.43 +/- 0.038 mg/aphid) over 24 h than symbiotic aphids (0.79) +/- 0.079 mg/aphid), but this difference was attributed primarily to the greater body size of the symbiotic aphids, suggesting that feeding by these larval aphids was not substantially impaired, The aposymbiotic larvae produced smaller honeydew droplets more frequently than symbiotic larvae, and no difference between the number of droplets produced in the first and second 12 h in the 24 h recording period was found, Aposymbiotic adults, in contrast, fed relatively poorly, Both EPG and honeydew production studies indicated that all symbiotic adults, but only 60-66% of aposymbiotic adults, had initiated phloem ingestion within a 10 h test period, It is proposed that the deleterious effects of bacterial disruption may be cumulative, and become increasingly severe and nonspecific with time since antibiotic treatment, It is recommended that studies on the nutritional physiology of aposymbiotic aphids are conducted with recently-generated aposymbionts, whose feeding responses are not impaired.TNArticle TL Wilkinson, Univ York, Dept Biol, York YO1 5DD, N Yorkshire, England ™Acyrthosiphon pisum; symbiose; Buchnera; miellat, HOMOPTERA; RƒSISTANCE; milieu artificiel, mŽtabolisme, puceron, aphide, EPG, Vicia faba, aposymbiotiqued Wiseman, B.R. Bondari, K.  1995B> endobj 3 0 obj << /Last 4 133 R >> endobj 4 133 obj << >> endobj 272 0 obj << >> endobj 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Gatehouse, A.M.R.ª 1996¦vEffects of GNA and other mannose binding lectins on development and fecundity of the potato-peach aphid Myzus persicae h Entomol. exp. appl.d79285-293 .'Entomologia Experimentalis et Applicata›Ni 0269¤ž$lectin, mode d'action, mannose, inhibition de croissance, Myzus persicae, insecte, binding, milieu artificial, toxicite, modelisation, rm, NPA, GNA, ASA, RSA JIP2,Sauvion, N. Charles, H. Febvay, G. RahbŽ, Y. 2004®}Effects of jackbean lectin (ConA) on the feeding behaviour and kinetics of intoxication of the pea aphid, Acyrthosiphon pisumÿ ÿj ÿ.'Entomologia Experimentalis et Applicata 110Ð 31-44pô°lectine, Concanavalin A, EPG, actography, Homoptera, Aphididae, midgut, plante transgŽnique, tube digestif, mŽtabolisme, pea aphid, Acyrthosiphon pisum, binding, mode d'action, ÿ„ N™ yD=Sauvion, N. Nardon, C. Febvay, G. Gatehouse, A.M.R. RahbŽ, Y.Ó 2004àœBinding of the insecticidal lectin Concanavalin A in pea aphid, Acyrthosiphon pisum (Harris) and induced effects on the structure of midgut epithelial cells Ö@ ÿS ÿ"Journal of Insect Physiology5012 1137-1150ið¬lectine, Concanavalin A, physiologie, Homoptera, Aphididae, midgut, plante transgŽnique, tube digestif, mŽtabolisme, pea aphid, Acyrthosiphon pisum, binding, mode d'action, Ö€ h• i("RA98, article, acceptŽ le 20/10/04