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PEDS Advance Access published online on January 25, 2006
Protein Engineering Design and Selection, doi:10.1093/protein/gzj009
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received July 15, 2005
Revised November 15, 2005
Accepted December 13, 2005

Article

Redesigning Bacillus thuringiensis Cry1Aa toxin into a mosquito toxin

Xinyan Sylvia Liu 1 and Donald H. Dean 1 *

1 Department of Biochemistry, The Ohio State University, Columbus, OH 43210-1292, USA

* To whom correspondence should be addressed.
Donald H. Dean, E-mail: dean.10{at}osu.edu


  Abstract

The Bacillus thuringiensis crystal protein Cry1Aa is normally selectively active to caterpillar larvae. Through rational design, toxicity (µg/ml) to the mosquito Culex pipiens was introduced by selected deletions and substitutions of the loop residues of domain II. Toxicity to its natural target Manduca sexta was concomitantly abolished. The successful grafting of the alternate mosquito toxicity onto the original lepidopteran Cry1Aa toxin demonstrates the possibility of designing and engineering a desired toxicity into any toxin of a common scaffold by reshaping the receptor binding region with desired specificities.

Keywords: mosquito; protein engineering.
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