期刊
JOURNAL OF INSECT PHYSIOLOGY
卷 55, 期 8, 页码 686-693出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jinsphys.2009.05.001
关键词
Bacillus thuringiensis; Cadherin; Cry1Ac toxin; Toxicity; Reduction
资金
- Ministry of Science and Technology [2006CB102004]
- Postdoctoral Science Foundation of China [20070420445]
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. (C) 2009 Elsevier Ltd. All rights reserved.
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