Cry11Aa of Bacillus thuringiensis subsp. israelensis is the most active toxin to Aedes aegypti in this strain. We previously reported that, in addition to a 65 kDa GPI (glycosylphosphatidylinositol)-anchored ALP (alkaline phosphatase), the toxin also binds a 250 kDa membrane protein. Since this protein is the same size as cadherin, which in lepidopteran insects is an important Cry toxin receptor, we developed an anti-AaeCad antibody. This antibody detects a 250 kDa protein in immunoblots of larval BBMVs (brush border membrane vesicles). The antibody inhibits Cry11Aa toxin binding to BBMVs and immunolocalizes the cadherin protein to apical membranes of distal and proximal caecae and posterior midgut epithelial cells. This localization is consistent with areas to which Cry11Aa toxin binds and causes pathogenicity. Therefore, the full-length Aedes cadherin cDNA was isolated from Aedes larvae and partial overlapping fragments that covered the entire protein were expressed in Escherichia coli. Using toxin overlay assays, we showed that one cadherin fragment, which contains CR7–11 (cadherin repeats 7–11), bound Cry11Aa and this binding was primarily through toxin domain II loops α8 and 2. Cadherin repeats CR8–11 but not CR7 bound Cry11Aa under non-denaturing conditions. Cry11Aa bound the cadherin fragment with high affinity with an apparent Kd of 16.7 nM. Finally we showed that this Cry11Aa-binding site could also be competed by Cry11Ba and Cry4Aa but not Cry4Ba. These results indicate that Aedes cadherin is possibly a receptor for Cry11A and, together with its ability to bind an ALP, suggest a similar mechanism of toxin action as previously proposed for lepidopteran insects.
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Research Article|
November 11 2009
Aedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis Available to Purchase
Jianwu Chen;
Jianwu Chen
*Department of Cell Biology and Neuroscience, University of California Riverside, Riverside, CA 92521, U.S.A.
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Karlygash G. Aimanova;
Karlygash G. Aimanova
*Department of Cell Biology and Neuroscience, University of California Riverside, Riverside, CA 92521, U.S.A.
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Luisa E. Fernandez;
Luisa E. Fernandez
†Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. postal 510-3, Cuernavaca 62250, Morelos, Mexico
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Alejandra Bravo;
Alejandra Bravo
†Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. postal 510-3, Cuernavaca 62250, Morelos, Mexico
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Mario Soberon;
Mario Soberon
†Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. postal 510-3, Cuernavaca 62250, Morelos, Mexico
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Sarjeet S. Gill
Sarjeet S. Gill
1
*Department of Cell Biology and Neuroscience, University of California Riverside, Riverside, CA 92521, U.S.A.
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
May 11 2009
Revision Received:
August 18 2009
Accepted:
September 04 2009
Accepted Manuscript online:
September 04 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 424 (2): 191–200.
Article history
Received:
May 11 2009
Revision Received:
August 18 2009
Accepted:
September 04 2009
Accepted Manuscript online:
September 04 2009
Citation
Jianwu Chen, Karlygash G. Aimanova, Luisa E. Fernandez, Alejandra Bravo, Mario Soberon, Sarjeet S. Gill; Aedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis. Biochem J 1 December 2009; 424 (2): 191–200. doi: https://doi.org/10.1042/BJ20090730
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