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Appl. Environ. Microbiol., 01 1996, 279-282, Vol 62, No. 1
MG Wolfersberger, XJ Chen and DH Dean
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.
Copyright © 1996, American Society for Microbiology
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
Department of Biology, Temple University, Philadelphia, Pennsylvania 19122, USA.
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