Molecular cloning of a cysteine proteinase cDNA from the cotton boll weevil Anthonomus grandis (Coleoptera: Curculionidae)

Bioscience, Biotechnology and Biochemistry

Volumn 68, Issue 6, 2004, Pages 1235-1242

  De Oliveira Neto, Osmundo Brilhante ^a,b   Batista, João Aguiar Nogueira ^a   Rigden, Daniel John ^a   Franco, Octávio Luiz ^a,c   Fragoso, Rodrigo Rocha ^a,b   Monteiro, Ana Carolina Santos ^a   Monnerat, Rose Gomes ^a   Grossi De Sá, Maria Fátima ^a  

^a EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA   (Brazil)

^b UNIVERSITY OF BRASILIA   (Brazil)

^c UNIVERSIDADE CATÓLICA DE BRASÍLIA   (Brazil)

Author keywords

Anthonomus grandis; cDNA cloning; Cotton boll weevil; Cysteine proteinase; Plant defense

Indexed keywords

COMPLEMENTARY DNA; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; MESSENGER RNA;

ANIMAL; ARTICLE; ENZYMOLOGY; GENETICS; LARVA; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE ALIGNMENT; TISSUE DISTRIBUTION; WEEVIL;

ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DNA, COMPLEMENTARY; LARVA; MOLECULAR SEQUENCE DATA; RNA, MESSENGER; SEQUENCE ALIGNMENT; TISSUE DISTRIBUTION; WEEVILS;

ANTHONOMUS; ANTHONOMUS GRANDIS; COLEOPTERA; CURCULIONIDAE; GOSSYPIUM HIRSUTUM; INSECTA; INVERTEBRATA;

EID: 4544274071     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.1235     Document Type: Article

References (49)

1. Wolfson, J., and Murdock, L., Diversity in digestive proteinase activity among insects. J. Che. Ecol., 16, 1089-1102 (1990).
2. Murdock, L. L., Brookhart, G., Dunn, P. E., Foard, D. E., Kelly, S., Kitch, L., Shade, R. E., Shukle, R. H., and Wolfson, J. L., Cysteine digestive proteinases in coleoptera. Comp. Biochem. Physiol., 87B, 783-787 (1997).
3. Murdock, L. L., Brookhart, G., Dunn, P. E., Foard, D. E., Kelly, S., Kitch, L., Shade, R. H., Norman, M. R., and Houseman, J. G., Identification of cathepsin B, D and L in the larva midgut of Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae). Insect Biochem. Mol. Biol., 171, 377-381 (1990).
4. Xavier-Filho, J., and Coelho, A., Acid proteinase of Callosobruchus maculatus and proteinase inhibitors of Vigna unguiculata. Annual Meeting of American Society of Plant Physiology and Phytochemical Society of North American Plant Physiology, 65, 138 (1980).
5. Campos, F. A. P., Xavier-Filho, J., Silva, C. P., and Ary, M. B., Resolution and partial characterization of proteinases and alpha-amylases from midguts of larvae of the bruchid beetle Callosobruchus maculatus (F.). Comp. Biochem. Physiol., 92B, 51-57 (1989).
6. Wieman, K. F., and Nielsen, S. S., Isolation and partial characterization of a major gut proteinase from larval Acanthoscelides obtectus (Coleoptera, Bruchidae). Comp. Biochem. Physiol., 89B, 419-426 (1988).
7. Ryan, C. A., Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phyt., 28, 425-440 (1990).
8. Hilder, V. A., Gatehouse, A. M. R., and Boulter, D., Transgenic plants conferring insect tolerance: protease inhibitor approach. In "Transgenic Plants", D Academic Press, New York, pp. 317-338 (1993).
9. Reeck, G. R., Kramer, K. J., Baker, J. E., Kanost, M. R., Fabrick, J. A., and Behnke, C. A., Proteinase inhibitors and resistance of transgenic plants to insects. In "Advances in Insect Control: The Role of Transgenic Plants", eds. Carozzi, N., and Koziel, M. G., Taylor and Francis, London, pp. 157-183 (1997).
10. Hilder, V., Gatehouse, A., Sheerman, S., Barker, R., and Boulter, D., A novel mechanism of insect resistance engineered into tobacco. Nature, 330, 160-163 (1987).
11. Johnson, R., Narvaez, J., Gyheung, A., and Ryan, C. A., Expression of proteinases inhibitors I and II in transgenic tobacco plants: effects on natural defense against Manduca sexta larvae. Proc. Natl. Acad. Sci. USA, 86, 9871-9875 (1989).
12. McManus, M. T., White, D. W. R., and McGregor, P. G., Accumulation of a chymotrypsin inhibitor in transgenic tobacco can affect the growth of insect pests. Transgenic Res., 3, 50-58 (1994).
13. Duan, X., Li, X., Xue, Q., Abo-el-Saad, M., Xu, D., and Wu, R., Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant. Nat. Biotechnol., 14, 494-498 (1996).
14. Xu, D. P., Xue, Q. Z., McElroy, D., Mawal, Y., Hilder, V. A., and Wu, R., Constitutive expression of a cowpea trypsin-inhibitor gene, CpTI, in transgenic rice plants confers resistance to 2 major rice insect pests. Mol. Breed., 2, 167-173 (1996).
15. Yeh, K. W., Lin, M. I., Tuan, S. J., Chen, Y. M., Lin, C. Y., and Kao, S. S., Sweet potato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura. Plant Cell Rep., 16, 686-699 (1997).
16. Xavier-Filho, J., The biological roles of serine and cysteine proteinase inhibitors in plants. Braz. J. Plant Physiol., 4, 1-6 (1992).
17. Liang, C., Brookmart, G., Feng, G. H., Reeck, G. R., and Kramer, K. J., Inhibition of digestive proteinase of stored grains Coleoptera by oryzacystatin, a cysteine proteinase inhibitor from rice seeds. FEBS Lett., 278, 139-142 (1991).
18. Michaud, D., Nguyen-Quoc, B., and Yelle, S., Selective inhibition of Colorado potato beetle cathepsin H by oryzacystatins I and II. FEBS Lett., 331, 173-176 (1993).
19. Chen, M., Johnson, B., Wen, L., Muthukrisnan, S., Kramer, K., Morgan, T., and Reeck, G., Rice cystatin: bacterial expression, purification, cysteine proteinase inhibitory activity and insect growth suppressing activity of a truncated form of the protein. Protein Expr. Purif., 3, 41-49 (1991).
20. Orr, G., Strickland, J., and Walsh, T., Inhibition of Diabrotica larval growth by multicystatin from potato tubers. J. Insect Physiol, 40, 893-900 (1994).
21. Edmonds, H. S., Gatehouse, L. N., Milder, V. A., and Gatehouse, J. A., The antimetabolic effects of oryzacystatin on larvae of the southern corn rootworm (Diabrotica undecimpunctata howardi): use of a bacterial expression system for oryzacystatin. Entomol. Exp. Appl., 78, 83-94 (1996).
22. Leplé, J. C., Bonadé-Bottino, M., Augustin, S., and Pilate, G., Toxicity to Chrysomela tremulae (Coleoptera:Chrysomelidae) of transgenic poplars expressing a cysteine proteinase inhibitor. Mol. Breed., 1, 319-328 (1995).
23. Takanashi, N., Kurata, S., and Natori, S., Molecular cloning of cDNA for the 29 kDa proteinase participating in decomposition of the larval fat body during metamorphosis of Sarcophaga peregrina (flesh fly). FEBS Lett., 334, 153-157 (1993).
24. Monnerat, R. G., Dias, S. C., Oliveira Neto, O. B., Nobre, S. D., Silva-Werneck, J. O., and Grossi-de-Sá, M. F., Criação massal do bicudo-do-algodoeiro Anthonomus grandis em laboratorio (Mass rearing of cotton boll weevil Anthonomus grandis in the laboratory). In "Comunicado Técnico Embrapa Recursos Genéticos e Biotecnologia" (Technical report of Embrapa Genetic Resource and Biotechnology), ed. Dias, J. M. C. S., Brazil, pp. 1-4 (2000).
25. Oliveira, A. S., Pereira, R. A., Lima, L. M., Morais, A. A. H., Melo, F. R., Franco, O. L., Bloch, Jr., C., Grossi-de-Sá, M. F., and Sales, M. P., Activity toward bruchid pest of a Kunitz-type inhibitor from seeds of the algaroba tree (Prosopis juliflora D.C.). Pest Biochem. Physiol., 72, 122-132 (2002).
26. Fernandes, K. V., Sabelli, P. A., Barratt, D. H., Richardson, M., Xavier-Filho, J., and Shewry, P. R., The resistance of cowpea seeds to bruchid beetles is not related to levels of cysteine proteinase inhibitors. Plant Mol. Biol, 23, 215-219 (1993).
27. Monteiro, A. C. S., Abrahamson, M., Lima, A. P. C. A., Vannier-Santos, M. A., and Scharfstein, J., Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi. J. Cell Sci., 114, 3933-3942 (2002).
28. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
29. Franco, O. L., Rigden, D. J., Melo, F. R., Bloch Junior, C., Silva, C. P., and Grossi-de-Sá, M. F., Activity of wheat α-amylase inhibitors towards bruchid α-amylases and structural explanation of observed specificities. Eur. J. Biochem., 267, 2166-2173 (2000).
30. Solomon, M., Belenghi, B., Delledone, M., Menachem, E., and Levine, A., The involvement of cysteine proteinase and proteinase inhibitor genes in the regulation of programmed cell death in plants. Plant Cell, 11, 431-443 (1999).
31. Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: a laboratory manual, 2nd edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York (1989).
32. Fourney, R. M., Miyakoshi, J., Day III, R. S., and Paterson, M. C., Northern blotting: efficient RNA staining and transfer. Focus, 10, 5-7 (1988).
33. Pearson, W. R., and Lipman, D. J., Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA, 85, 2444-2448 (1988).
34. Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680 (1994).
35. Barton, G. J., ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng., 6, 37-40 (1993).
36. Franco, O. L., Grossi-de-Sá, M. F., Sales, M. F., Mello, L. V., Oliveira, A. S., and Rigden, D. J., Overlapping binding sites for trypsin and papain on a Kunitz-type proteinase inhibitor from Prosopis juliflora. Proteins, 49, 335-341 (2002).
37. Watanabe, H., Abe, K., Emori, Y., Hosoyama, H., and Arai, S., Molecular cloning and gibberellin-induced expression of multiple cysteine proteinase for rice seeds (oryzasins). J. Biol. Chem., 266, 16897-16902 (1991).
38. Rogers, J. C., Dean, D., and Heck, G. R., Aleurain: a barley thiol protease closely related to mammalian cathepsin H. Proc. Natl. Acad. Sci. USA, 82, 6512-6516 (1985).
39. Ishidoh, K., Imajoh, S., Emori, Y., Ohno, S., Kawasaki, H., Minami, Y., Kominami, E., Katunuma, N., and Suzuki, K., Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases. FEBS Lett., 226, 33-37 (1987).
40. Ishidoh, K., Towatari, T., Imajoh, S., Kawasaki, H., Kominami, E., Katunuma, N., and Suzuki, K., Molecular cloning and sequencing of cDNA for rat cathepsin L. FEBS Lett., 223, 69-73 (1987).
41. Cohen, L. W., Coghlan, V. M., and Dihel, L. C., Cloning and sequencing of papain-encoding cDNA. Gene, 48, 219-227 (1986).
42. San Segundo, B., Chan, S. J., and Steiner, D. F., Identification of cDNA clones encoding a precursor of rat liver cathepsin B. Proc. Natl. Acad. Sci. USA, 82, 2320-2324 (1985).
43. Kamphuis, I. G., Kalk, K. H., Swarte, M. B. A., and Drenth, J., Structure of papain refined at 1.65 Angstrom resolution. J. Mol. Biol., 179, 233-256 (1984).
44. Matsumoto, I., Watanabe, H., Abe, K., Arai, S., and Emori, Y., A putative digestive cysteine proteinase of an insect, Drosophila melanogaster, predominantly expressed in embryonic and larval midgut. Eur. J. Biol., 227, 582-587 (1995).
45. Barrett, A. J., and Rawlings, N. D., Families and clans of cysteine peptidases. Perspect. Drug. Discov. Design., 6, 1-11 (1996).
46. McGrath, M. E., The lysosomal cysteine proteases. Annu. Rev. Biophys. Biomol. Struct., 28, 181-204 (1999).
47. Guncar, G., Podobnik, M., Pungercar, J., Strukelj, B., Turk, V., and Turk, D., Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure, 6, 51-61 (1998).
48. McGrath, M. E., Klaus, J. L., Barnes, M. G., and Bromme, D., Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat. Struct. Biol., 4, 105-109 (1997).
49. Taylor, M. A., Baker, K. C., Briggs, G. S., Connerton, I. F., Cummings, N. J., Pratt, K. A., Revell, D. F., Freedman, R. B., and Goodenough, P. W., Recombinant pro-regions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes. Protein Eng., 8, 59-62 (1995).