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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/18981
Title: Amino acid substitutions in αA and αC of Cyt2Aa2 alter hemolytic activity and mosquito-larvicidal specificity
Authors: Boonhiang Promdonkoy
Amporn Rungrod
Patcharee Promdonkoy
Wanwarang Pathaichindachote
Chartchai Krittanai
Sakol Panyim
Thailand National Center for Genetic Engineering and Biotechnology
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 1-Feb-2008
Citation: Journal of Biotechnology. Vol.133, No.3 (2008), 287-293
Abstract: Cyt2Aa2 produced by Bacillus thuringiensis subsp. darmstadiensis exhibits in vitro cytolytic activity against broad range of cells but shows specific in vivo toxicity against larvae of Dipteran insects. To investigate the role of amino acids in αA and αC of this toxin, 3 single-point mutants (A61C, S108C and V109A) were generated. All 3 mutant proteins were highly produced as inclusion bodies that could be solubilized and activated by proteinase K similar to that of the wild type. Hemolytic activity of A61C and S108C mutants was significantly reduced whereas the V109A mutant showed comparable hemolytic activity to the wild type. Interestingly, the A61C mutant exhibited high larvicidal activity to both Aedes aegypti and Culex quinquefasciatus. S108C and V109A mutants showed low activity against C. quinquefasciatus but relatively high toxicity to A. aegypti. These results demonstrated for the first time that amino acids in αA and αC are involved in the selectivity of the Cyt toxin to the targeted organism. © 2007 Elsevier B.V. All rights reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=37448999135&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/18981
ISSN: 01681656
Appears in Collections:Scopus 2006-2010

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