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Amino acid substitutions in αA and αC of Cyt2Aa2 alter hemolytic activity and mosquito-larvicidal specificity

Paper ID Volume ID Publish Year Pages File Format Full-Text
24803 43538 2008 7 PDF Available
Title
Amino acid substitutions in αA and αC of Cyt2Aa2 alter hemolytic activity and mosquito-larvicidal specificity
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.

Keywords
Bacillus thuringiensis; Cyt toxin; Hemolytic; Larvicidal protein; Mosquito; Specificity determinant
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Amino acid substitutions in αA and αC of Cyt2Aa2 alter hemolytic activity and mosquito-larvicidal specificity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 133, Issue 3, 1 February 2008, Pages 287–293
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us