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PEDS Advance Access originally published online on January 25, 2006
Protein Engineering Design and Selection 2006 19(3):107-111; 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

Redesigning Bacillus thuringiensis Cry1Aa toxin into a mosquito toxin

Xinyan Sylvia Liu and Donald H. Dean1

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

1 To whom correspondence should be addressed. E-mail: dean.10{at}osu.edu

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

Received July 15, 2005; revised November 15, 2005; accepted December 13, 2005.

Edited by Mark Zoller


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