Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae)

被引:88
作者
Li, HR
Oppert, B
Higgins, RA
Huang, FN
Zhu, KY
Buschman, LL
机构
[1] USDA ARS, Grain Marketing & Prod Res Ctr, Manhattan, KS 66502 USA
[2] Kansas State Univ, Dept Entomol, Manhattan, KS 66506 USA
关键词
Bacillus thuringiensis; cry proteins; European corn borer; Ostrinia nubilalis; trypsin; chymotrypsin; elastase; resistance mechanisms;
D O I
10.1016/j.ibmb.2004.03.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Proteinase activities were compared in soluble and membrane fractions of guts obtained from larvae of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis. Overall, serine proteinases from soluble fractions of the susceptible strain were more active than those of the resistant strain. The soluble trypsin-like proteinase activity of the resistant strain was approximately half that of the susceptible strain. The number and relative molecular masses of soluble and membrane serine proteinases were different. However, there were no significant differences in the activities of serine proteinases and aminopeptidases extracted from midgut membranes of the two strains. Cry1Ab protoxin hydrolysis by soluble proteinase extracts of the resistant strain was reduced approximately 20-30% relative to that of the susceptible strain. Reduced protoxin processing due to decreased activities of Bt protoxin activation proteinases may be associated with resistance to Bt toxin in this resistant strain of O. nubilalis. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:753 / 762
页数:10
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