Activities of Bacillus thuringiensis insecticidal crystal proteins Cyt1Aa and Cyt2Aa against three species of sheep blowfly.
The toxicity of Bacillus thuringiensis Cyt1Aa protein to sheep blowfly larvae depends on its solubilization and proteolytic activation. Cyt1Aa crystals were not toxic. Full-length and trypsin-digested Cyt1Aa proteins were toxic to larvae of three species of sheep blowfly. Neither full-length nor trypsin-digested Cyt2A soluble crystal proteins were toxic.
Chilcott
C N
CN
BioDiscovery New Zealand Limited, Parnell, Auckland, New Zealand. cchilcott@biodiscovery.co.nz
Wigley
P J
PJ
Broadwell
A H
AH
Park
D J
DJ
Ellar
D J
DJ
D000818:Animals; D001413:Bacillus thuringiensis; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000633:toxicity*; D001427:Bacterial Toxins / Q000633:toxicity*; D004175:Diptera; D004731:Endotoxins / Q000633:toxicity*; D006460:Hemolysin Proteins; D007814:Larva; D010572:Pest Control, Biological; D012756:Sheep / Q000469:parasitology*
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis