Insecticidal Specificity of Cry1Ah to Helicoverpa armigera Is Determined by Binding of APN1 via Domain II Loops 2 and 3

文献类型： 外文期刊

第一作者： Liu, Yuxiao

作者： Liu, Yuxiao;Liang, Gemei;Song, Fuping;Zhou, Xueping;Zhang, Jie;Huang, Yongping;Bravo, Alejandra;Soberon, Mario

作者机构：

关键词： Bacillus thuringiensis;Cry1Ah;Cry1Ai;insecticidal specificity;Helicoverpa armigera;aminopeptidase N

期刊名称：APPLIED AND ENVIRONMENTAL MICROBIOLOGY （ 影响因子：4.792； 五年影响因子：5.26 ）

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收录情况： SCI

摘要： Bacillus thuringiensis Cry1Ah protein is highly toxic against Helicoverpa armigera but shows no toxicity against Bombyx mori larvae. In contrast, the closely related Cry1Ai toxin showed the opposite phenotype: high activity against B. mori but no toxicity against H. armigera. Analysis of binding of Cry1Ah to brush border membrane vesicle (BBMV) proteins from H. armigera and B. mori by surface plasmon resonance revealed association of toxin binding with insect specificity. Pulldown experiments identified aminopeptidase N1 (APN1) as a Cry1Ah binding protein that was not observed in the assays using B. mori BBMV proteins. The APN1 Cry1Ah binding region was narrowed to the region from (A)548 to (S)798 (fragment H3) by expressing four different APN1 fragments in Escherichia coli and analyzing Cry1Ah binding by ligand blot. Binding competition experiments of Cry1Ah to APN1 fragment H3 using synthetic peptides corresponding to four predicted domain II loop regions showed that loop 2 and loop 3 have additive effects on binding to APN1 fragment H3. Moreover, switching of loop 2 and loop 3 regions from Cry1Ah to Cry1Ai toxins showed that loop 2 and loop 3 are both involved in specificity and toxicity against H. armigera.

分类号： Q939.9`X1

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