Article
Efficient production of Bacillus thuringiensis Cry1AMod toxins under regulation of cry3Aa promoter and single cysteine mutations in the protoxin region.
Applied and environmental microbiology - 1 Nov 2013
García-Gómez Blanca I, Sánchez Jorge, Martínez de Castro Diana L, Ibarra Jorge E, Bravo Alejandra, Soberón Mario
Abstract excerpt
Bacillus thuringiensis Cry1AbMod toxins are engineered versions of Cry1Ab that lack the amino-terminal end, including domain I helix α-1 and part of helix α-2. This deletion improves oligomerization of these toxins in solution in the absence of cadherin receptor and counters resistance to Cry1A toxins in different lepidopteran insects, suggesting that oligomerization plays a major role in their toxicity. However,...
Topics
- Animals
- Bacillus thuringiensis
- Bacillus thuringiensis Toxins
- Bacterial Proteins
- Bacterial Toxins
- Cysteine
- DNA, Bacterial
- Endotoxins
- Escherichia coli
- Hemolysin Proteins