Article
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.
Applied and environmental microbiology - 1 Jan 1996
Wolfersberger M G, Chen X J, Dean D H
Abstract excerpt
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...
Topics
- Animals
- Arginine
- Bacillus thuringiensis
- Bacillus thuringiensis Toxins
- Bacterial Proteins
- Bacterial Toxins
- Bombyx
- Cell Membrane Permeability
- Endotoxins
- Hemolysin Proteins
- Larva
- Microvilli
- Mutagenesis, Site-Directed
- Mutation