Reduction of Bacillus thuringiensis Cry1Ac toxicity against Helicoverpa armigera by a soluble toxin-binding cadherin fragment

文献类型： 外文期刊

第一作者： Liu, Chenxi

作者： Liu, Chenxi;Wu, Kongming;Gao, Yulin;Ning, Changming;Wu, Yidong;Ning, Changming;Oppert, Brenda

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关键词： Helicoverpa armigera;Bacillus thuringiensis;crystal proteins;bacterial toxins;toxicity;cadherins;binding proteins;binding sites;binding capacity;midgut;epithelial cells;receptors

期刊名称：JOURNAL OF INSECT PHYSIOLOGY （ 影响因子：2.354； 五年影响因子：3.045 ）

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收录情况： SCI

摘要： A cadherin-like protein has been identified as a putative receptor for Bacillus thuringiensis (Bt) Cry1Ac toxin in Helicoverpa armigera and plays a key role in Bt insecticidal action. In this study, we produced a fragment from this H. armigera Cry1Ac toxin-binding cadherin that included the predicted toxin-binding region. Binding of Cry1Ac toxin to this cadherin fragment facilitated the formation of a 250-kDa toxin oligomer. The cadherin fragment was evaluated for its effect on Cry1Ac toxin-binding and toxicity by ligand blotting, binding assays, and bioassays. The results of ligand blotting and binding assays revealed that the binding of Cry1Ac to H. armigera midgut epithelial cells was reduced under denaturing or native conditions in vitro. Bioassay results indicated that toxicities from Cry1Ac protoxin or activated toxin were reduced in vivo by the H. armigera cadherin fragment. The addition of the cadherin fragment had no effect on Cry2Ab toxicity.

分类号： Q965

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