Enhancement of Cry19Aa mosquitocidal activity against Aedes aegypti by mutations in the putative loop regions of domain II.
Improvements in the mosquitocidal activity of Bacillus thuringiensis Cry19Aa were achieved by protein engineering of putative surface loop residues in domain II through rational design. The improvement of Aedes toxicity in Cry19Aa was 42,000-fold and did not affect its toxicity against Anopheles or Culex.
Abdullah
Mohd Amir F
MA
Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Dean
Donald H
DH
D000330:Aedes / Q000187:drug effects*; D000595:Amino Acid Sequence; D000818:Animals; D001413:Bacillus thuringiensis / Q000378:metabolism; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000633:toxicity*; D001427:Bacterial Toxins / Q000737:chemistry* / Q000235:genetics / Q000633:toxicity*; D004731:Endotoxins / Q000737:chemistry* / Q000235:genetics / Q000633:toxicity*; D006460:Hemolysin Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010572:Pest Control, Biological; D015202:Protein Engineering / Q000379:methods*
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis