Abstract
Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa competed for those of Vip3Af.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Bacillus thuringiensis / physiology*
-
Bacillus thuringiensis Toxins
-
Bacterial Proteins / metabolism*
-
Bacterial Proteins / toxicity
-
Endotoxins / metabolism*
-
Endotoxins / toxicity
-
Gastrointestinal Tract / microbiology*
-
Hemolysin Proteins / metabolism*
-
Hemolysin Proteins / toxicity
-
Larva / drug effects
-
Lethal Dose 50
-
Protein Binding
-
Spodoptera / microbiology*
Substances
-
Bacillus thuringiensis Toxins
-
Bacterial Proteins
-
Endotoxins
-
Hemolysin Proteins
-
Vip3A protein, Bacillus thuringiensis
-
insecticidal crystal protein, Bacillus Thuringiensis