Activity of Bacillus thuringiensis delta-endotoxins against codling moth (Cydia pomonella L.) larvae.
Solubilized protoxins of nine Cry1 and one hybrid Cry1 delta-endotoxin from Bacillus thuringiensis were tested for their activity against larvae of the codling moth (Cydia pomonella L). Cry1Da was the most toxic, followed by Cry1Ab, Cry1Ba, and Cry1Ac, while Cry1Aa, Cry1Fa, Cry1Ia, and SN19 were still less active. Cry1Ca and Cry1Cb showed no activity. In vitro trypsin activation increased activity of all eight active delta-endotoxins, and dramatically enhanced toxicity of hybrid SN19, Cry1Aa, Cry1Ac, and Cry1Fa. The differences between toxicity of proteins before and after trypsin digestion suggests that proteolytic activation in the C. pomonella digestive tract plays a critical role for the activity of Cry proteins against this insect.
Boncheva
Rumyana
R
University of Plovdiv "Paisii Hilendarski", 4000 Plovdiv, Bulgaria.
Dukiandjiev
Stefan
S
Minkov
Ivan
I
de Maagd
Ruud A
RA
Naimov
Samir
S
D000818:Animals; D001413:Bacillus thuringiensis; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000145:classification / Q000494:pharmacology; D001427:Bacterial Toxins / Q000145:classification / Q000494:pharmacology; D004731:Endotoxins / Q000145:classification / Q000494:pharmacology; D006460:Hemolysin Proteins; D007300:Insect Control; D007306:Insecticides; D007814:Larva / Q000254:growth & development; D009036:Moths; D010572:Pest Control, Biological / Q000379:methods
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D007306:Insecticides; C030956:insecticidal crystal protein, Bacillus Thuringiensis