Redesigning Bacillus thuringiensis Cry1Aa toxin into a mosquito toxin.
The Bacillus thuringiensis crystal protein Cry1Aa is normally selectively active to caterpillar larvae. Through rational design, toxicity (microg/ml) to the mosquito Culex pipiens was introduced by selected deletions and substitutions of the loop residues of domain II. Toxicity to its natural target Manduca sexta was concomitantly abolished. The successful grafting of the alternate mosquito toxicity onto the original lepidopteran Cry1Aa toxin demonstrates the possibility of designing and engineering a desired toxicity into any toxin of a common scaffold by reshaping the receptor binding region with desired specificities.
Liu
Xinyan Sylvia
XS
Department of Biochemistry, The Ohio State University, Columbus, 43210-1292, USA.
Dean
Donald H
DH
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001413:Bacillus thuringiensis / Q000235:genetics*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism / Q000633:toxicity*; D001427:Bacterial Toxins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism / Q000633:toxicity*; D001681:Biological Assay; D002942:Circular Dichroism; D003465:Culex / Q000382:microbiology*; D004731:Endotoxins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism / Q000633:toxicity*; D017353:Gene Deletion; D006460:Hemolysin Proteins; D007814:Larva / Q000382:microbiology; D018402:Manduca; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010572:Pest Control, Biological; D015202:Protein Engineering; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis