The toxicity test and hypothetical model of Bacillus thuringiensis Cry1Aa helix4

文献类型： 外文期刊

第一作者： Qu, H

作者： Qu, H;Vachon, V;Luo, J;Zhang, J;Laprade, R;Zhu, Y

作者机构：

关键词： Bt toxin proteins;light scattered assay;ion channel;molecular model

期刊名称：SCIENCE IN CHINA SERIES C-LIFE SCIENCES （ 影响因子：1.61； 五年影响因子：1.148 ）

ISSN： 1006-9305

年卷期： 2002 年 45 卷 6 期

页码：

收录情况： SCI

摘要： Development of targeted biological agents against agricultural insect pests is of prime importance for the elaboration and implementation of integrated pest management strategies that are environment-friendly, respectful of bio-diversity and safer to human health through reduced use of chemical pesticides. A major goal to understand how Bt toxins work is to elucidate the functions of their three domains. Domains II and III are involved in binding specificity and structural integrity, but the function of Domain I remains poorly understood. Using a Manduca sexta BBMV (brush border membrane vesicles) system, we analyzed its responses to Cry1Aa 15 single-point mutations with altered Domain I helix 4 residues. Light scattering assay showed that toxicity was almost lost in 3 mutants, and we observed significantly reduced toxicity in other 7 mutants. However, 5 mutants retained wild-type toxicity. Using computer software, we simulated the three-dimensional structures of helix 4. Both experimental and bioinformatic analysis showed that residues in Cry1Aa Domain I helix 4 were involved in the formation of ion channels that is critical for its insect toxicity.

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