Concanavalin A inhibits development of tomato moth (Lacanobia oleracea) and peach-potato aphid (Myzus persicae) when expressed in transgenic potato plants
Molecular Breeding - 1999
Tóm tắt
The effects of concanavalin A (ConA), a glucose/mannose-specific lectin from jackbean (Canavalia ensiformis), on insect crop pests from two different orders, Lepidoptera and Homoptera, were investigated. When fed to larvae of tomato moth (Lacanobia oleracea) at a range of concentrations (0.02–2.0% of total protein) in artificial diet, ConA decreased survival, with up to 90% mortality observed at the highest dose level, and retarded development, but had only a small effect on larval weight. When fed to peach-potato aphids (Myzus persicae) at a range of concentrations (1–9μM) in liquid artificial diet, ConA reduced aphid size by up to 30%, retarded development to maturity, and reduced fecundity (production of offspring) by >35%, but had little effect on survival. With both insects, there was a poor correlation between lectin dose and the quantitative effect. Constitutive expression of ConA in transgenic potatoes driven by the CaMV 35S promoter resulted in the protein accumulating to levels lower than predicted, possibly due to potato not being able to adequately reproduce the post-translational processing of this lectin which occurs in jackbean. However, the expressed lectin was functionally active as a haemagglutinin. Bioassay of L. oleracea larvae on ConA-expressing potato plants showed that the lectin retarded larval development, and decreased larval weights by >45%, but had no significant effect on survival. It also decreased consumption of plant tissue by the larvae. In agreement with the diet bioassay results, ConA-expressing potatoes decreased the fecundity of M. persicae by up to 45%. ConA thus has potential as a protective agent against insect pests in transgenic crops.
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Tài liệu tham khảo
Bevan M: Agrobacterium vectors for plant transformation. Nucl Acids Res 12: 8711–8721 (1984).
Boulter D, Edwards GA, Gatehouse AMR, Gatehouse JA, Hilder VA: Additive protective effects of incorporating two different higher plant derived insect resistance genes in transgenic tobacco plants. Crop Prot 9: 351–354 (1990).
Bowles DJ, Marcus SE, Pappin DJC, Findlay JBC, Eliopoulos E, Maycox PR, Burgess J: Posttranslational processing of concanavalin-A precursors in jackbean cotyledons. J Cell Biol 102: 1284–1297 (1986).
Chrispeels MJ, Raikhel NV: Lectins, lectin genes, and their role in plant defence. Plant Cell 3: 1–9 (1991).
Czalpa TH, Lang BA: Effect of plant lectins on the larval development of European corn borer (Lepidoptera: Pyralidae) and southern corn rootwirm (Coleoptera: Chrysomelidae). J Econ Entomol 83: 2480–2485 (1990).
Devonshire AL: Insecticide resistance in Myzus persicae; from field to gene and back again. Pesticide Sci 26: 375–382 (1989).
Down RE, Gatehouse AMR, Hamilton WDO, Gatehouse JA: Snowdrop lectin inhibits development and fecundity of the glasshouse potato aphid (Aulacorthum solani) when administered in vitro and via transgenic plants, both in laboratory and glasshouse trials. J Insect Physiol 42: 1035–1045 (1996).
Eisemann CH, Donaldson RA, Pearson RD, Cadagon LC, Vuocolo T, Tellam RL: Larvicidal activity of lectins on Lucilla cuprina: mechanism of action. Entomol Exp Appl 72: 1–11 (1994).
Ellis THN, Davies DR, Castleton JA, Bedford ID: The organisation and genetics of rDNA length variants in peas. Chromosoma 91: 74–81 (1984).
Fitches E, Gatehouse AMR, gatehouse JA: 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. J Insect Physiol, in press (1997).
Gatehouse AMR, Davison GM, Newell CA, Merryweather A, Hamilton WDO, Burgess EPJ, Gilbert RJC, Gatehouse JA: Transgenic potato plants with enhanced resistance to the tomato moth Lacanobia oleracea; growthroom trials. Mol Breed 3: 49–63 (1997).
Gatehouse AMR, Dewey FM, Dove J, Fenton KA, Pusztai A: Effect of seed lectin from Phaseolus vulgaris on the larvae of Callosobruchus maculatus; mechanism of toxicity. J Sci Food Agric 35: 373–380 (1984).
Gatehouse AMR, Down RE, Powell KS, Sauvion N, Rahbé Y, Newell CA, Merryweather A, Gatehouse JA: Effects of GNAexpressing transgenic potato plants on peach-potato aphid, Myzus persicae. Entomol Exp Appl 79: 295–307 (1996).
Gatehouse AMR, Gatehouse JA: Identifying proteins with insecticidal activity: Use of encoding genes. Pesticide Sci 52: 165–175 (1998).
Gatehouse AMR, Powell KS, Peumans WJ, Van Damme EJM, Gatehouse JA: Insecticidal properties of lectins: Their potential in plant protection. In: Pusztai AJ, Bardocz S (ed) Lectins: Biomedical Perspectives, pp. 35–57, Taylor and Francis, Hants., UK (1995).
Gatehouse AMR, Shackley SJ, Fenton KA, Bryden J, Pusztai A: Mechanism of seed lectin tolerance by a major insect storage pest of Phaseolus vulgaris, Acanthoscelides obtectus. J Sci Food Agric 47: 269–280 (1989).
Habibi J, Backus EA, Czalpa TH: Plant lectins affect survival of the potato leafhopper. J Econ Entomol 86: 945–951 (1993).
Hill DS: Agricultural pests of temperate regions and their control. Cambridge University Press, Cambridge, UK (1987).
Honeyborne CHB: An investigation of the responses of aphids to plants treated with growth regulators. Ph.D. thesis, University of Reading, UK (1969).
Jongsma MA, Bolter C: The adaptation of insects to plant proteinase inhibitors. Plant Physiol 43: 885–895 (1997).
Jouanin L, Bonade-Bottino M, Girard C, Morrot G, Giband M: Transgenic plants for insect resistance. Plant Sci 131: 1–11 (1998).
Kumar A: Agrobacterium-mediated transformation of potato genotypes. In: Gartland KV, Davey MR (eds) Methods in Molecular Biology: Agrobacterium Protocols, pp. 121–128. Humana Press, USA (1995).
Licastro F, Davis LJ, Morini MC: Lectins and superantigens: membrane interactions of these compounds with T lymphocytes affect immune responses. Int J Biochem 25: 845–852 (1993).
Lis H, Sharon N: The biochemistry of plant lectins (phytohaemagglutinins). Annu Rev Biochem 42: 541–574 (1973).
Min W, Dunn AJ, Jones DH: Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage. EMBO J 11: 1303–1307 (1992).
Moreno J, Chrispeels MJ: A lectin gene encodes the-amylase inhibitor of common bean. Proc Natl Acad Sci USA 86: 7885–7889 (1989).
Murdock LL, Huesing JE, Nielsen SS, Pratt RC, Shade RE: Biological effects of plant lectins on the cowpea weevil. Phytochemistry 29: 85–89 (1990).
Peumans WJ, Van Damme EJM: Lectins as plant defense proteins. Plant Physiol 109: 347–352 (1995).
Powell KS, Gatehouse AMR, Hilder VA, Gatehouse JA: Antimetabolic effects of plant lectins and fungal enzymes on the nymphal stages of two important rice pests, Nilaparvata lugens and Nephotettix cinciteps. Entomol Exp Appl 66: 119–126 (1993).
Powell KS, Gatehouse AMR, Hilder VA, Gatehouse JA: Antifeedant effects of plant lectins and enzymes on the adult stage of the rice brown planthopper, Nilaparvata lugens. Entomol Exp Appl 75: 51–59 (1995).
Powell KS, Gatehouse AMR, Hilder VA, van Damme EJM, Peumans WJ, Boonjawat J, Horsham K, Gatehouse JA: Different antimetabolic effects of related lectins towards nymphal stages of Nilaparvata lugens. Entomol Exp Appl 75: 61–65 (1995).
Powell KS, Spence J, Bharathi M, Gatehouse JA, Gatehouse AMR: Immunohistochemical and developmental studies to elucidate the mechanism of action of the snowdrop lectin on the rice brown planthopper, Nilaparvata lugens (Stal). J Insect Physiol 44: 529–539 (1998).
Pusztai A: Plant Lectins. Cambridge University Press, Cambridge, UK (1991).
Pusztai A, Grant G, Ewen SWB, Peumans WJ, Van Damme EJM, Bardocz S: Infection of the gut by pathogenic bacteria is inhibited by dietary lectins: chemical probiosis. In: Pusztai AJ, Bardocz S (eds) Lectins: Biomedical Perspectives, pp. 313–322, Taylor and Francis, Hants., UK (1995).
Rahbé Y, Febvay G: Protein toxicity to aphids: an in vitro test on Acyrthosiphon pisum. Entomol Exp Appl 67: 149–160 (1993).
Rahbé Y, Sauvion N, Febvay G, Peumans WJ, Gatehouse AMR: Toxicity of lectins and processing of ingested proteins in the pea aphid Acyrthosiphon pisum. Entomol Exp Appl 76: 143–155 (1995).
Rao KV, Rathore KS, Hodges TK, Fu X, Stoger E, Sudhakar D, Williams S, Christou P, Bharathi M, Bown DP, Powell KS, Spence J, Gatehouse AMR, Gatehouse JA: Expression of snowdrop lectin (GNA) in the phloem of transgenic rice plants confers resistance to rice brown planthopper. Plant J 15: 469–477 (1998).
Sauvion N, Rahbé Y, Peumans WJ, van Damme E, Gatehouse JA, Gatehouse AMR: Effects of GNA and other mannosebinding lectins on development and fecundity of the peachpotato aphid. Entomol Exp Appl 79: 285–293 (1996).
Schuler TH, Poppy GM, Kerry BR, Denholm I: Insectresistant transgenic plants. Trends Biotechnol 16: 168–175 (1998).
Shade RE, Schroeder HE, Pueto JJ, Tabe LM, Murdock LL, Higgins TJV, Chrispeels MJ: Transgenic pea seeds expressing the alpha amylase inhibitor of the common bean are resistant to bruchid beetles. Bio/technology 12: 793–796 (1994).
Sheldon PS, Bowles DJ: The glycoprotein precursor of concanavalin-A is converted to an active lectin by deglycosylation. EMBO J 11: 1297–1301 (1992).
Sheldon PS, Keen JN, Bowles DJ: Post-translational peptide bond formation during concanavalin A processing in vitro. Biochem J 320: 865–870 (1996).
Shukle RH, Murdock LL: Lipoxygenase, trypsin inhibitor and lectin from soybeans: effects on larval growth of Manduca sexta (Lepidoptera: Sphingidae). Environ Entomol 12: 787–791 (1983).
Stoger E, Williams S, Christou P, Down RE, Gatehouse JA: Expression of the insecticidal lectin from snowdrop (Galanthus nivalis agglutinin; GNA) in transgenic wheat plants: effects on predation by the grain aphid Sitobion avenae. Mol Breed, in press (1998).