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Bacillus thuringiensis Vip3 mutant proteins: Insecticidal activity and trypsin sensitivity

文献类型： 外文期刊

作者： Li, Chunyu 1 ; Xu, Ning 2 ; Huang, Xiaoping 2 ; Wang, Wei 3 ; Cheng, Jiaan; Wu, Kongming; Shen, Zhicheng;

作者机构： 1.Zhejiang Univ, Inst Insect Sci, Hangzhou 310029, Peoples R China

2.Zhejiang Univ, Inst Insect Sci, Hangzhou 310029, Peoples R China; Zhejiang Univ, State Key Lab Rice Biol, Hangzhou 310029, Peoples R China; Guangdong Acad Agr Sci, Inst Fruit Tree Res, Guangzhou, Guangdong, Peoples R China; Chinese Acad Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing, Peoples R China

3.Zhejiang Univ, Inst Insect Sci, Hangzhou 310029, Peoples R China; Zhejiang Univ, State Key Lab Rice Biol, Hangzhou 310029, Peoples R China; Guangdong Acad Agr Sci, Inst Fruit Tree Res, Guangzhou, Guangdong, Peoples R China; Chinese Acad Sci, Inst Plant Protect, State Key Lab Biol Plant Dis &

关键词： bacillus thuringiensis;Vip3;insecticidal protein;Vip3 mutantstrypsin

期刊名称：BIOCONTROL SCIENCE AND TECHNOLOGY （ 影响因子：1.665； 五年影响因子：1.616 ）

ISSN： 0958-3157

年卷期： 2007 年 17 卷 7 期

页码：

收录情况： SCI

摘要： Vip3 is a novel insect toxin isolated from Bacillus thuringiensis (Bt), and could be used as an alternative toxin for Bt delta-endotoxins for transgenic insect control. Vip3 mutants with deletion, addition or mutations at the very end of the C-terminus were generated. The deletion and addition of a few amino acid residues at the C-terminus totally abolished the insecticidal activity. The mutation of the last two residues from IK to LG also resulted in the total loss of its insecticidal activity; however, the mutation from IK to LR increased its activity substantially against beet armyworm. Interestingly, all the inactive mutants were found to be highly sensitive to trypsin digestion, while the active mutant generated a trypsin-resistant polypeptide of 62-kDa upon trypsin digestion. However, this 62-kDa polypeptide expressed in E. coli from the 5' end truncated vip3 gene was biologically inactive and sensitive to trypsin digestion. Thus, the N-terminal part of the protein is required to form the 62-kDa trypsin resistant core. This study suggested that the 62-kDa peptide core could be a hallmark of active insecticidal Vip3 proteins.

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