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Journal Article | Research Support, U.S. Gov't, P.H.S.

Site-directed mutations in the third domain of Bacillus thuringiensis delta-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles.

M G Wolfersberger, X J Chen, D H Dean
M G Wolfersberger
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X J Chen
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D H Dean
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ABSTRACT

A series of mutant Bacillus thuringiensis CryIAa delta-endotoxin proteins was prepared by replacing the first, second, and last arginine residues of the conserved third-domain sequence, R-521 YRVRIR-527, with other amino acids. The stable mutant proteins were bioassayed against Bombyx mori larvae and found to all be approximately half as active as wild-type CryIAa. The toxins were also tested by means of a light-scattering assay for their ability to increase permeability of larval B. mori midgut brush border membrane vesicles. Three of the mutant toxins were as active as the wild-type toxin in the vesicle permeability assay.

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Site-directed mutations in the third domain of Bacillus thuringiensis delta-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles.
M G Wolfersberger, X J Chen, D H Dean
Applied and Environmental Microbiology Jan 1996, 62 (1) 279-282; DOI:

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Site-directed mutations in the third domain of Bacillus thuringiensis delta-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles.
M G Wolfersberger, X J Chen, D H Dean
Applied and Environmental Microbiology Jan 1996, 62 (1) 279-282; DOI:
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