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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/33405
Title: Functional characterizations of residues Arg-158 and Tyr-170 of the mosquito-larvicidal Bacillus thuringiensis Cry4Ba
Authors: Somphob Leetachewa
Saengduen Moonsom
Urai Chaisri
Narumol Khomkhum
Nonglak Yoonim
Ping Wang
Chanan Angsuthanasombat
Mahidol University
Western University
Cornell University New York State Agricultural Experiment Station
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2014
Citation: BMB Reports. Vol.47, No.10 (2014), 546-551
Abstract: © 2014 by the The Korean Society for Biochemistry and Molecular Biology. The insecticidal activity of Bacillus thuringiensis (Bt) Cry toxins involves toxin stabilization, oligomerization, passage across the peritrophic membrane (PM), binding to midgut receptors and pore-formation. The residues Arg-158 and Tyr-170 have been shown to be crucial for the toxicity of Bt Cry4Ba. We characterized the biological function of these residues. In mosquito larvae, the mutants R158A/E/Q (R158) could hardly penetrate the PM due to a significantly reduced ability to alter PM permeability; the mutant Y170A, however, could pass through the PM, but degraded in the space between the PM and the midgut epithelium. Further characterization by oligomerization demonstrated that Arg-158 mutants failed to form correctly sized high-molecular weight oligomers. This is the first report that Arg-158 plays a role in the formation of Cry4Ba oligomers, which are essential for toxin passage across the PM. Tyr-170, meanwhile, is involved in toxin stabilization in the toxic mechanism of Cry4Ba in mosquito larvae.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84908879241&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/33405
ISSN: 1976670X
19766696
Appears in Collections:Scopus 2011-2015

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