| Literature DB >> 18054404 |
Boonhiang Promdonkoy1, Amporn Rungrod, Patcharee Promdonkoy, Wanwarang Pathaichindachote, Chartchai Krittanai, Sakol Panyim.
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 alphaA and alphaC 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 alphaA and alphaC are involved in the selectivity of the Cyt toxin to the targeted organism.Entities:
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Year: 2007 PMID： 18054404 DOI： 10.1016/j.jbiotec.2007.10.007
Source DB: PubMed Journal: J Biotechnol ISSN： 0168-1656 Impact factor: 3.307