메뉴 건너뛰기




Volumn 97, Issue 6, 2004, Pages 2095-2100

Soyacystatin N inhibits proteolysis of wheat α-amylase inhibitor and potentiates toxicity against cowpea weevil

Author keywords

C. maculatus; Cysteine protease inhibitor; Synergistic effect; amylase inhibitor

Indexed keywords

CALLOSOBRUCHUS; CALLOSOBRUCHUS MACULATES; CALLOSOBRUCHUS MACULATUS; COLEOPTERA; GLYCINE MAX; HEXAPODA; INSECTA; TRITICUM AESTIVUM;

EID: 12344290714     PISSN: 00220493     EISSN: None     Source Type: Journal    
DOI: 10.1093/jee/97.6.2095     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin): Homology with animal cystatins and transient expression in the ripening process of rice seeds
    • Abe, K., Y. Emori, H. Kondo, K. Suzuki, and S. Arai. 1987. Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin): homology with animal cystatins and transient expression in the ripening process of rice seeds. J. Biol. Chem. 262: 16793-16797.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 2
    • 0000420912 scopus 로고
    • Additive protective effects of different plant-derived insect resistance genes in transgenic tobacco plants
    • Boulter, D., G. A. Edwards, A.M.R. Gatehouse, J. A. Gatehouse, and V. A. Hilder. 1990. Additive protective effects of different plant-derived insect resistance genes in transgenic tobacco plants. Crop Protection 9: 351-354.
    • (1990) Crop Protection , vol.9 , pp. 351-354
    • Boulter, D.1    Edwards, G.A.2    Gatehouse, A.M.R.3    Gatehouse, J.A.4    Hilder, V.A.5
  • 3
    • 0000549241 scopus 로고
    • Resolution and partial characterization of proteinases and alpha-amylases from midguts of larvae of the bruchid beetle Callosobruchus maculatus (F.)
    • Campos, F.A.P., J. Xavier, C. P. Silva, and M. B. Ary. 1989. Resolution and partial characterization of proteinases and alpha-amylases from midguts of larvae of the bruchid beetle Callosobruchus maculatus (F.). Comp. Biochem. Physiol. B 92: 51-57.
    • (1989) Comp. Biochem. Physiol. B , vol.92 , pp. 51-57
    • Campos, F.A.P.1    Xavier, J.2    Silva, C.P.3    Ary, M.B.4
  • 4
    • 0347297183 scopus 로고    scopus 로고
    • Broccoli plants with pyramided cry1Ac and cry1C Bt genes control diamondback moths resistant to Cry1A and Cry1C proteins
    • Cao, J., J. Z. Zhao, J. D. Tang, A. M. Shelton, and E. D. Earle. 2002. Broccoli plants with pyramided cry1Ac and cry1C Bt genes control diamondback moths resistant to Cry1A and Cry1C proteins. Theor. Appl. Genet. 105: 258-264.
    • (2002) Theor. Appl. Genet. , vol.105 , pp. 258-264
    • Cao, J.1    Zhao, J.Z.2    Tang, J.D.3    Shelton, A.M.4    Earle, E.D.5
  • 6
    • 6744237863 scopus 로고
    • Presence and partial characterization of a major proteolytic-enzyme in the larval gut of Callosobruchus maculates
    • Gatehouse, A.M.R., K. J. Butler, K. A. Fenton, and J. A. Gatehouse. 1985. Presence and partial characterization of a major proteolytic-enzyme in the larval gut of Callosobruchus maculates. Entomol. Exp. Appl. 39: 279-286.
    • (1985) Entomol. Exp. Appl. , vol.39 , pp. 279-286
    • Gatehouse, A.M.R.1    Butler, K.J.2    Fenton, K.A.3    Gatehouse, J.A.4
  • 7
    • 84985427919 scopus 로고
    • The effects of alpha-amylase inhibitors on insect storage pests - Inhibition of alpha-amylase in vitro and effects on development in vivo
    • Gatehouse, A.M.R., K. A. Fenton, I. Jepson, and D. J. Pavey. 1986. The effects of alpha-amylase inhibitors on insect storage pests - inhibition of alpha-amylase in vitro and effects on development in vivo. J. Sci. Food Agric. 37: 727-734.
    • (1986) J. Sci. Food Agric. , vol.37 , pp. 727-734
    • Gatehouse, A.M.R.1    Fenton, K.A.2    Jepson, I.3    Pavey, D.J.4
  • 8
    • 0025596105 scopus 로고
    • The effect of two proteinase inhibitors, E-64 and Bowman-Birk trypsin inhibitor, on the developmental time and mortality of Acanthoscelides obtectus (Say)
    • Hines, M. E., S. S. Nielsen, R. E. Shade, and M. A. Pomeroy. 1990. The effect of two proteinase inhibitors, E-64 and Bowman-Birk trypsin inhibitor, on the developmental time and mortality of Acanthoscelides obtectus (Say). Entomol. Exp. Appl. 57: 201-207.
    • (1990) Entomol. Exp. Appl. , vol.57 , pp. 201-207
    • Hines, M.E.1    Nielsen, S.S.2    Shade, R.E.3    Pomeroy, M.A.4
  • 9
    • 12044251220 scopus 로고
    • alpha-Amylase inhibitor, not phytohemagglutinin, explains resistance of common bean-seeds to cowpea weevil
    • Huesing, J. E., R. E. Shade, M. J. Chrispeels, and L. L. Murdock. 1991. alpha-Amylase inhibitor, not phytohemagglutinin, explains resistance of common bean-seeds to cowpea weevil. Plant Physiol. 96: 993-996.
    • (1991) Plant Physiol. , vol.96 , pp. 993-996
    • Huesing, J.E.1    Shade, R.E.2    Chrispeels, M.J.3    Murdock, L.L.4
  • 10
    • 85008573096 scopus 로고
    • Growth inhibitory effects of alpha-amylase inhibitor from the kidney bean, Phaseolus vulgaris (L) on 3 species of bruchids (Coleoptera, Bruchidae)
    • Ishimoto, M., and K. Kitamura. 1989. Growth inhibitory effects of alpha-amylase inhibitor from the kidney bean, Phaseolus vulgaris (L) on 3 species of bruchids (Coleoptera, Bruchidae). Appl. Entomol. Zool. 24: 281-286.
    • (1989) Appl. Entomol. Zool. , vol.24 , pp. 281-286
    • Ishimoto, M.1    Kitamura, K.2
  • 11
    • 0029848547 scopus 로고    scopus 로고
    • Bruchid resistance of transgenic azuki bean expressing seed alpha-amylase inhibitor of common bean
    • Ishimoto, M., T. Sato, M. J. Chrispeels, and K. Kitamura. 1996. Bruchid resistance of transgenic azuki bean expressing seed alpha-amylase inhibitor of common bean. Entomol. Exp. Appl. 79: 309-315.
    • (1996) Entomol. Exp. Appl. , vol.79 , pp. 309-315
    • Ishimoto, M.1    Sato, T.2    Chrispeels, M.J.3    Kitamura, K.4
  • 12
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • Jongsma, M. A., and C. Bolter. 1997. The adaptation of insects to plant protease inhibitors. J. Insect Physiol. 43: 885-895.
    • (1997) J. Insect Physiol. , vol.43 , pp. 885-895
    • Jongsma, M.A.1    Bolter, C.2
  • 13
    • 84990439459 scopus 로고
    • Partial characterization of a major gut thiol proteinase from larvae of Callosobruchus maculatus F
    • Kitch, L. W., and L. L. Murdock. 1986. Partial characterization of a major gut thiol proteinase from larvae of Callosobruchus maculatus F. Arch. Insect Biochem. 3: 561-575.
    • (1986) Arch. Insect Biochem. , vol.3 , pp. 561-575
    • Kitch, L.W.1    Murdock, L.L.2
  • 17
    • 0035094826 scopus 로고    scopus 로고
    • Expression of multiple insecticidal genes confers broad resistance against a range of different rice pests
    • Maqbool, S. B., S. Riazuddin, N. T. Loc, A.M.R. Gatehouse, J. A. Gatehouse, and P. Christou. 2001. Expression of multiple insecticidal genes confers broad resistance against a range of different rice pests. Mol. Breed. 7: 85-93.
    • (2001) Mol. Breed. , vol.7 , pp. 85-93
    • Maqbool, S.B.1    Riazuddin, S.2    Loc, N.T.3    Gatehouse, A.M.R.4    Gatehouse, J.A.5    Christou, P.6
  • 18
    • 0029682164 scopus 로고    scopus 로고
    • Response of digestive cysteine proteinases from the Colorado potato beetle (Leptinotarsa decemlineata) and the black vine weevil (Otiorynchus sulcatus) to a recombinant form of human stefin A
    • Michaud, D., B. NguyenQuoc, T. C. Vrain, D. Fong, and S. Yelle. 1996. Response of digestive cysteine proteinases from the Colorado potato beetle (Leptinotarsa decemlineata) and the black vine weevil (Otiorynchus sulcatus) to a recombinant form of human stefin A. Arch. Insect Biochem. Physiol. 31: 451-464.
    • (1996) Arch. Insect Biochem. Physiol. , vol.31 , pp. 451-464
    • Michaud, D.1    NguyenQuoc, B.2    Vrain, T.C.3    Fong, D.4    Yelle, S.5
  • 19
    • 0001591343 scopus 로고
    • Effects of E-64, a cysteine proteinase-inhibitor, on cowpea weevil growth, development, and fecundity
    • Murdock, L. L., R. E. Shade, and M. A. Pomeroy. 1988. Effects of E-64, a cysteine proteinase-inhibitor, on cowpea weevil growth, development, and fecundity. Environ. Entomol. 17: 467-469.
    • (1988) Environ. Entomol. , vol.17 , pp. 467-469
    • Murdock, L.L.1    Shade, R.E.2    Pomeroy, M.A.3
  • 20
    • 0027170847 scopus 로고
    • Dietary mixtures of cysteine and serine proteinase-inhibitors exhibit synergistic toxicity toward the red flour beetle, Tribolium castaneum
    • Oppert, B., T. D. Morgan, C. Culbertson, and K. J. Kramer. 1993. Dietary mixtures of cysteine and serine proteinase-inhibitors exhibit synergistic toxicity toward the red flour beetle, Tribolium castaneum. Comp. Biochem. Physiol. C 105: 379-385.
    • (1993) Comp. Biochem. Physiol. C , vol.105 , pp. 379-385
    • Oppert, B.1    Morgan, T.D.2    Culbertson, C.3    Kramer, K.J.4
  • 21
    • 0000259353 scopus 로고
    • Inhibition of Diabrotica larval growth by a multicystatin from potato tubers
    • Orr, G. L., J. A. Strickland, and T. A. Walsh. 1994. Inhibition of Diabrotica larval growth by a multicystatin from potato tubers. J. Insect Physiol. 40: 893-900.
    • (1994) J. Insect Physiol. , vol.40 , pp. 893-900
    • Orr, G.L.1    Strickland, J.A.2    Walsh, T.A.3
  • 22
    • 0002965916 scopus 로고
    • Selection of biotype population-2 and population-3 of Nilaparvata lugens (Homoptera, Delphacidae) by exposure to resistant rice varieties
    • Pathak, P. K., and E. A. Heinrichs. 1982. Selection of biotype population-2 and population-3 of Nilaparvata lugens (Homoptera, Delphacidae) by exposure to resistant rice varieties. Environ. Entomol. 11: 85-90.
    • (1982) Environ. Entomol. , vol.11 , pp. 85-90
    • Pathak, P.K.1    Heinrichs, E.A.2
  • 23
    • 0001107258 scopus 로고    scopus 로고
    • Greenbug (Homoptera: Aphididae) biotypes: Selected by resistant cultivars or preadapted opportunists?
    • Porter, D. R., J. D. Burd, K. A. Shufran, J. A. Webster, and G. L. Teetes. 1997. Greenbug (Homoptera: Aphididae) biotypes: selected by resistant cultivars or preadapted opportunists? J. Econ. Entomol. 90: 1055-1065.
    • (1997) J. Econ. Entomol. , vol.90 , pp. 1055-1065
    • Porter, D.R.1    Burd, J.D.2    Shufran, K.A.3    Webster, J.A.4    Teetes, G.L.5
  • 25
    • 0032578732 scopus 로고    scopus 로고
    • Two-toxin strategies for management of insecticidal transgenic crops: Can pyramiding succeed where pesticide mixtures have not?
    • Roush, R. T. 1998. Two-toxin strategies for management of insecticidal transgenic crops: can pyramiding succeed where pesticide mixtures have not? Phil. Trans. R. Soc. B 353: 1777-1786.
    • (1998) Phil. Trans. R. Soc. B , vol.353 , pp. 1777-1786
    • Roush, R.T.1
  • 27
    • 0000401178 scopus 로고
    • Artificial seed system for bioassay of cowpea weevil (Coleoptera, Bruchidae) growth and development
    • Shade, R. E., L. L. Murdock, D. E. Foard, & M. A. Pomeroy. 1986. Artificial seed system for bioassay of cowpea weevil (Coleoptera, Bruchidae) growth and development. Environ. Entomol. 15: 1286-1291.
    • (1986) Environ. Entomol. , vol.15 , pp. 1286-1291
    • Shade, R.E.1    Murdock, L.L.2    Foard, D.E.3    Pomeroy, M.A.4
  • 28
    • 0028041555 scopus 로고
    • Transgenic pea-seeds expressing the alpha-amylase inhibitor of the common bean are resistant to bruchid beetles
    • Shade, R. E., H. E. Schroeder, J .J. Pueyo, L. M. Tabe, L. L. Murdock, T.J.V. Higgins, and M. J. Chrispeels. (1994). Transgenic pea-seeds expressing the alpha-amylase inhibitor of the common bean are resistant to bruchid beetles. BioTechnology 12: 793-796.
    • (1994) BioTechnology , vol.12 , pp. 793-796
    • Shade, R.E.1    Schroeder, H.E.2    Pueyo, J.J.3    Tabe, L.M.4    Murdock, L.L.5    Higgins, T.J.V.6    Chrispeels, M.J.7
  • 29
    • 0000833695 scopus 로고
    • Distribution, ecology and importance of bruchids attacking grain legumes and pulses in Africa
    • Taylor, T. 1981. Distribution, ecology and importance of bruchids attacking grain legumes and pulses in Africa. Ser. Entomol. 19: 199.
    • (1981) Ser. Entomol. , vol.19 , pp. 199
    • Taylor, T.1
  • 30
    • 0027691245 scopus 로고
    • Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor
    • Waldron, C., L. M. Wegrich, P.A.O. Merlo, and T. A. Walsh. 1993. Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor. Plant Mol. Biol. 23: 801-812.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 801-812
    • Waldron, C.1    Wegrich, L.M.2    Merlo, P.A.O.3    Walsh, T.A.4
  • 31
    • 0027740380 scopus 로고
    • Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains
    • Walsh, T. A., and J. A. Strickland. 1993. Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains. Plant Physiol. 103: 1227-1234.
    • (1993) Plant Physiol. , vol.103 , pp. 1227-1234
    • Walsh, T.A.1    Strickland, J.A.2
  • 32
    • 0030220996 scopus 로고    scopus 로고
    • Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog
    • Zhao, Y., M. A. Botella, L. Subramanian, X. Niu, S. S. Nielsen, R. A. Bressan, and P. M. Hasegawa. 1996. Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol. 111: 1299-1306.
    • (1996) Plant Physiol. , vol.111 , pp. 1299-1306
    • Zhao, Y.1    Botella, M.A.2    Subramanian, L.3    Niu, X.4    Nielsen, S.S.5    Bressan, R.A.6    Hasegawa, P.M.7
  • 33
    • 0344154314 scopus 로고    scopus 로고
    • Fusion of a soybean cysteine protease inhibitor and a legume lectin enhances anti-insect activity synergistically
    • Zhu-Salzman, K., J.-E. Ahn, R. A. Salzman, H. Koiwa, R. E. Shade, and S. Balfe. 2003a. Fusion of a soybean cysteine protease inhibitor and a legume lectin enhances anti-insect activity synergistically. Agric. For. Entomol. 5:317-323.
    • (2003) Agric. For. Entomol. , vol.5 , pp. 317-323
    • Zhu-Salzman, K.1    Ahn, J.-E.2    Salzman, R.A.3    Koiwa, H.4    Shade, R.E.5    Balfe, S.6
  • 34
    • 0345146929 scopus 로고    scopus 로고
    • Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor
    • Zhu-Salzman, K., H. Koiwa, R. A. Salzman, R. E. Shade, and J-E. Ahn. 2003b. Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor. Insect Mol. Biol. 12: 135-145.
    • (2003) Insect Mol. Biol. , vol.12 , pp. 135-145
    • Zhu-Salzman, K.1    Koiwa, H.2    Salzman, R.A.3    Shade, R.E.4    Ahn, J.-E.5
  • 35
    • 0035488307 scopus 로고    scopus 로고
    • Functional mechanics of the plant defensive Griffonia simplicifolia lectin II: Resistance to proteolysis is independent of glycoconjugate binding in the insect gut
    • Zhu-Salzman, K., and R. A. Salzman. 2001. Functional mechanics of the plant defensive Griffonia simplicifolia lectin II: Resistance to proteolysis is independent of glycoconjugate binding in the insect gut. J. Econ. Entomol. 94: 1280-1284.
    • (2001) J. Econ. Entomol. , vol.94 , pp. 1280-1284
    • Zhu-Salzman, K.1    Salzman, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.