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Reduction of Bacillus thuringiensis Cry1Ac toxicity against Helicoverpa armigera by a soluble toxin-binding cadherin fragment.
J Insect Physiol. 2009 Aug; 55(8):686-93.JI

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.

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Authors+Show Affiliations

Liu C
State Key Laboratory of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Wu K
No affiliation info available
Wu Y
No affiliation info available
Gao Y
No affiliation info available
Ning C
No affiliation info available
Oppert B
No affiliation info available

MeSH

AnimalsBacillus thuringiensis ToxinsBacterial ProteinsCadherinsEndotoxinsHemolysin ProteinsInsect ProteinsInsecticidesMothsProtein BindingSolubility

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19446559

Citation

Liu, Chenxi, et al. "Reduction of Bacillus Thuringiensis Cry1Ac Toxicity Against Helicoverpa Armigera By a Soluble Toxin-binding Cadherin Fragment." Journal of Insect Physiology, vol. 55, no. 8, 2009, pp. 686-93.
Liu C, Wu K, Wu Y, et al. Reduction of Bacillus thuringiensis Cry1Ac toxicity against Helicoverpa armigera by a soluble toxin-binding cadherin fragment. J Insect Physiol. 2009;55(8):686-93.
Liu, C., Wu, K., Wu, Y., Gao, Y., Ning, C., & Oppert, B. (2009). Reduction of Bacillus thuringiensis Cry1Ac toxicity against Helicoverpa armigera by a soluble toxin-binding cadherin fragment. Journal of Insect Physiology, 55(8), 686-93. https://doi.org/10.1016/j.jinsphys.2009.05.001
Liu C, et al. Reduction of Bacillus Thuringiensis Cry1Ac Toxicity Against Helicoverpa Armigera By a Soluble Toxin-binding Cadherin Fragment. J Insect Physiol. 2009;55(8):686-93. PubMed PMID: 19446559.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Reduction of Bacillus thuringiensis Cry1Ac toxicity against Helicoverpa armigera by a soluble toxin-binding cadherin fragment. AU - Liu,Chenxi, AU - Wu,Kongming, AU - Wu,Yidong, AU - Gao,Yulin, AU - Ning,Changming, AU - Oppert,Brenda, Y1 - 2009/05/26/ PY - 2009/03/20/received PY - 2009/05/02/revised PY - 2009/05/04/accepted PY - 2009/5/19/entrez PY - 2009/5/19/pubmed PY - 2009/9/9/medline SP - 686 EP - 93 JF - Journal of insect physiology JO - J Insect Physiol VL - 55 IS - 8 N2 - 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. SN - 1879-1611 UR - https://www.unboundmedicine.com/medline/citation/19446559/Reduction_of_Bacillus_thuringiensis_Cry1Ac_toxicity_against_Helicoverpa_armigera_by_a_soluble_toxin_binding_cadherin_fragment_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-1910(09)00205-4 DB - PRIME DP - Unbound Medicine ER -