Bacillus thuringiensis Cry2Ab is active on Anopheles mosquitoes: Single D block exchanges reveal critical residues involved in activity

FEMS Microbiology Letters

Volumn 325, Issue 1, 2011, Pages 16-21

  Mcneil, Betina C ^a   Dean, Donald H ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Mosquitocidal proteins; Mutagenic analysis; Protein engineering

Indexed keywords

BACTERIAL TOXIN; CRY2AA TOXIN; CRY2AB TOXIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANOPHELES GAMBIAE; ARTICLE; BACILLUS THURINGIENSIS; BIOLOGICAL CONTROL AGENT; CONTROLLED STUDY; INSECTICIDAL ACTIVITY; LC 50; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RECEPTOR BINDING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TOXIN ANALYSIS; WILD TYPE;

AEDES; ANIMALS; ANOPHELES GAMBIAE; BACTERIAL PROTEINS; CULEX; ENDOTOXINS; HEMOLYSIN PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

ANOPHELES (GENUS); ANOPHELES GAMBIAE; BACILLUS THURINGIENSIS; DIPTERA; LEPIDOPTERA;

EID: 80755167730     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02403.x     Document Type: Article

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