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Reduction of Bacillus thuringiensis Cry1Ac toxicity against Helicoverpa armigera by a soluble toxin-binding cadherin fragment |
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| Authors: | Chenxi Liu Yidong Wu Changming Ning Brenda Oppert |
| Affiliation: | a State Key Laboratory of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China b Department of Entomology, College of Plant Protection, Nanjing Agricultural University, Nanjing, 210095, China c Department of Entomology, College of Agronomy and Biotechnology, China Agricultural University, Beijing, 100193, China d USDA ARS Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502, USA |
| Abstract: | 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. |
| Keywords: | Bacillus thuringiensis Cadherin Cry1Ac toxin Toxicity Reduction |
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