Pesticidal and receptor binding properties of Bacillus thuringiensis Cry1Ab and Cry1Ac delta-endotoxin mutants to Pectinophora gossypiella and Helicoverpa zea.

doi:10.1007/s002840010163

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Article

Pesticidal and receptor binding properties of Bacillus thuringiensis Cry1Ab and Cry1Ac delta-endotoxin mutants to Pectinophora gossypiella and Helicoverpa zea.

Current microbiology - 1 Dec 2000

Karim S, Dean D H

Abstract excerpt

Bacillus thuringiensis produces several larvicidal crystalline inclusions during sporulation. An understanding of their mechanisms of action is commercially important. In this study, two toxins, Cry1Ab and Cry1Ac, were compared that showed 98% amino acid identity in domain I and II, but differed significantly in domain III. Using site-directed mutagenesis techniques, two conserved loop 2 Arg's ((368)RR(369)) of...

Topics

Animals
Bacillus thuringiensis
Bacillus thuringiensis Toxins
Bacterial Proteins
Bacterial Toxins
Binding Sites
Binding, Competitive
Endotoxins
Hemolysin Proteins
Insect Control
Insect Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Insecticides

Moths

Mutation

Pest Control, Biological

Protein Binding

Protein Structure, Tertiary

Receptors, Cell Surface

Source

Open in PubMed

Identifiers

PMID: 11080394
DOI: 10.1007/s002840010163

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