Protein digestibility, protease activity, and post-embryonic development of the velvetbean caterpillar (Anticarsia gemmatalis) exposed to the trypsin-inhibitor benzamidine

Pesticide Biochemistry and Physiology

Volumn 86, Issue 1, 2006, Pages 23-29

  Pilon, Anderson M ^a   Oliveira, Maria Goreti A ^a   Guedes, Raul Narciso C ^a  

^a FEDERAL UNIVERSITY OF VIÇOSA   (Brazil)

Author keywords

Adaptation to protease inhibitors; Insect digestion; Noctuidae; Protease inhibition; Serine proteases

Indexed keywords

ANTICARSIA GEMMATALIS; HEXAPODA; INSECTA; LEPIDOPTERA; MUCUNA DEERINGIANA; NOCTUIDAE;

EID: 33746750830     PISSN: 00483575     EISSN: 10959939     Source Type: Journal    
DOI: 10.1016/j.pestbp.2005.11.005     Document Type: Article

References (44)

1. Bernays E.A., and Chapman R.F. Host-Plant Selection by Phytophagous Insects (1994), Chapman & Hall, New York p. 312
2. Stotz H.U., Kroymann J., and Mitchell-Olds T. Plant-insect interactions. Curr. Opin. Plant Biol. 2 (1999) 268-272
3. Carlini C.R., and Grossi-de-Sá M.F. Plant toxic proteins with inseticidal properties. A review on their potentialities as bioinseticides. Toxicon 40 (2000) 1515-1539
4. Ryan C.A. Genes for improving defences against insects and pathogens. Annu. Rev. Phytopathol. 28 (1990) 245-449
5. Felton G.W., and Gatehouse J.A. Antinutritive plant defence mechanisms. In: Lehane M.J., and Billingsley P.F. (Eds). Biology of the Insect Midgut (1996), Chapman & Hall, New York 373-416
6. Hilder V.A., Gatehouse A.M.R., Sheerman S.E., Barker R.F., and Boulter D. A novel mechanism of insect resistance engineered into tobacco. Nature 330 (1987) 160-163
7. Boulter D. Insect pest control by copying nature using genetically engineered crops. Phytochemistry 34 (1993) 1453-1466
8. Hilder V.A., and Boulter D. Genetic engineering of crop plants for insect resistance-a critical review. Crop Prot. 18 (1999) 177-191
9. Oliveira M.G.A., De Simone S.G., Xavier L.P., and Guedes R.N.C. Partial purification and characterization of digestive trypsin-like proteases from the velvet bean caterpillar, Anticarsia gemmatalis. Comp. Biochem. Physiol. B 140 (2005) 369-380
10. Xavier L.P., Oliveira M.G.A., Guedes R.N.C., Santos A.V., and De Simone S.G. Trypsin-like activity of membrane-bound midgut proteases from Anticarsia gemmatalis (Lepidoptera: Noctuidae). Eur. J. Entomol. 102 (2005) 139-145
11. Gatehouse A.M.R., and Gatehouse J.A. Identifying proteins with insecticidal activity: use of encoding genes to produce insect-resistant transgenic crops. Pestic. Sci. 52 (1998) 165-175
12. Jouanin L., Bonadé-Bottino M., Girard C., Morrot G., and Giband M. Transgenic plants for insect resistance. Plant Sci. 131 (1998) 1-11
13. Mares-Guia M., Rogana E., Amorin A.F., and Magalhães-Rocha N.M. Kinetic evidence for a two-state hybrid model for the trypsin activation by modifiers. J. Biol. Chem. 256 (1981) 1661-1668
14. Applebaum S.W. Biochemistry of digestion. In: Kerkut G.A., and Gilbert L.L. (Eds). Comprehensive Insect Physiology, Biochemistry and Pharmacology vol. 4 (1986), Pergamon Press, New York 279-311
15. Terra W.R., and Ferreira C. Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. B 109 (1994) 1-62
16. Reeck G.R., Oppert B., Denton M., Kanost M., Baker J.E., and Kramer K.J. Insect proteinases. In: Turk V. (Ed). Proteases: New Perspectives (1999), Birkauzer Verlag, Boston 125-148
17. Ma C.C., and Kanost M.R. A beta 1,3-glucan recognition protein from an insect, Manduca sexta agglutinates microorganisms and activates the phenoloxidase cascade. J. Biol. Chem. 275 (2000) 7505-7514
18. Gormam M.J., and Paskewitz S.M. Serine proteases as mediators of mosquito immune response. Insect Biochem.Mol. Biol. 31 (2001) 257-262
19. Lam W., Coast G.M., and Rayne R.C. Characterization of multiple trypsins from the midgut of Locusta migratoria. Insect Biochem. Mol. Biol. 30 (2000) 85-94
20. Birk Y. Plant Protease Inhibitors (2003), Springer, Berlin p. 170
21. Broadway R.M. Are insects resistant to plant proteinase inhibitors?. J. Insect Physiol. 41 (1995) 107-116
22. Jongsma M.A., Bakker P.L., Peters J., Bosch D., and Stickema W.J. Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of proteinase activity insensitive to inhibition. Proc. Natl. Acad. Sci. USA 92 (1995) 8041-8045
23. Jongsma M.A., Stiekema W.J., and Bosch D. Combatting inhibitor-insensitive proteases of insect pests. Trends Biotechnol. 14 (1996) 331-333
24. Jongsma M.A., and Bolter C. The adaptation of insects to plant protease inhibitors. J. Insect Physiol. 43 (1997) 885-895
25. Michaud D. Avoiding protease-mediated resistance in herbivorous pests. Trends Biotechnol. 15 (1997) 4-6
26. Paulillo L.C.M.S., Lopes A.R., Cristofoletti P.T., Parra J.R.P., Terra W.R., and Silva-Filho M. Changes in midgut endopeptidase activity of Spodoptera frugiperda (Lepidoptera: Noctuidae) are responsible for adaptation to soybean proteinase inhibitors. J. Econ. Entomol. 93 (2000) 892-896
27. Brito L.O., Lopes A.R., Parra J.R.P., Terra W.R., and Silva-Filho M.C. Adaptation of tobacco budworm Heliothis virescens to proteinase inhibitors may be mediated by the synthesis of new proteinases. Comp. Biochem. Physiol. 128B (2001) 365-375
28. Zhu-Salzman K., Koiwa H., Salzman R.A., Shades R.E., and Ahn J.E. Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor. Insect Mol. Biol. 12 (2003) 135-145
29. Bown D.P., Wilkinson H.S., and Gatehouse J.A. Regulation of expression of genes encoding digestive proteases in the gut of a polyphagous lepidopteran larva in response to dietary protease inhibitors. Physiol. Entomol. 29 (2004) 278-290
30. Silva F.B., Oliveira M.G.A., Batista R.B., Pires C.V., Xavier L.P., Piovesan N.D., Oliveira J.A., José I.C., and Moreira M.A. Função fisiológica de lipoxigenases de folhas de soja submetidas ao ataque de lagarta (Anticarsia gemmatalis Hübner). Arq. Inst. Biol. 60 (2002) 67-74
31. D. Gallo, O. Nakano, S. Silveira Neto, R.P.L. Carvalho, G.C. Baptista, E. Berti Filho, J.R.P. Parra, R.A. Zucchi, S.B. Alves, J.D. Vendramim, L.C. Marchini, J.L.S. Lopes, C. Omoto, Entomologia Agrícola, FEALQ, Piracicaba, 2001, p. 871.
32. C.B. Hoffman-Campo, E.B. Oliveira, F. Moscardi, Criação Massal de Lagarta da Soja (Anticarsia gemmatalis), Documentos 10, EMBRAPA-CNPSo, Londrina, 1985, p. 32.
33. Instituto Adolfo Lutz, Normas Analíticas do Instituto Adolfo Lutz-Métodos Químicos e Físicos para Análise de Alimentos, vol. 1, third ed., IAL, São Paulo, 1985, p. 254.
34. Sykes P. Guidebook to Mechanism in Organic Chemistry. sixth ed. (1996), Prentice Hall, Upper Saddle, NJ
35. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
36. Kunitz M. Crystalline soybean trypsin inhibitor. II-General properties. J. Gen. Physiol. 30 (1947) 291-310
37. Erlanger B.F., Kokowsky N., and Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95 (1961) 271-278
38. SAS Institute, SAS/STAT User's Guide: Statistics, version 6.12, SAS Institute, Cary, NC, USA.
39. von Ende C.N. Repeated-measures analysis: growth and other time-dependent measures. In: Scheiner S., and Gurevitch J. (Eds). Design and Analysis of Ecological Experiments (1993), Chapman & Hall, New York 113-137
40. Koiwa H., Bressan R.A., and Hasegawa P.M. Regulation of protease inhibitors and plant defense. Trends Plant Sci. 2 (1997) 379-384
41. Broadway R.M., and Duffey S.S. Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua. J. Insect Physiol. 32 (1986) 827-833
42. De Leo F., Bonade-Bottino M.A., Ceci L.R., Gallerani R., and Jouanin L. Opposite effects on Spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants. Plant Physiol. 118 (1998) 997-1004
43. Mazumdar-Leighton S., and Broadway R.M. Transcriptional induction of diverse midgut trypsins in larval Agrotis ipsilon and Helicoverpa zea feeding on the soybean trypsin inhibitor. Insect Biochem. Mol. Biol. 31 (2001) 645-657
44. Oliveira M.G.A., Rogana E., Rosa J.C., Reinhold B.B., Andrade M.H., Greene L.J., and Mares-Guia M. Tyrosine 151 is part of the substrate activation binding site. J. Biol. Chem. 268 (1993) 26893-26903