Development and mechanisms of resistance to Bacillus thuringiensis endotoxin Cry1Ac in the American bollworm, Helicoverpa armigera (Hübner).
The American bollworm, H. armigera, evolved 31-fold resistance to selection pressure of B. thuringiensis endotoxin Cry1Ac within six generations. The Cry1Ac selected larvae of H. armigera showed cross-resistance to Cry1Aa and Cry1Ab both in terms of mortality and growth reduction. Studies on mechanisms of resistance to Cry1Ac showed that proteases of resistant insects degraded Cry1Ac faster than those of susceptible insects, which led to the relative unavailability of toxin of about 58 kDa for binding and perforation of midgut epithelial membrane of the target insect. Besides, resistant and susceptible populations of H. armigera differed in the binding of their receptors with Cry1Ac toxin. These results suggest the possibility of both mechanisms existing in imparting resistance. These findings mandate the necessity of B. thuringiensis resistance management for usage of B. thuringiensis either as a conventional insecticide or through transgenic crops.
Chandrashekar
K
K
Division of Entomology, Indian Agricultural Research Institute, New Delhi 110 012, India.
Gujar
G T
GT
D000818:Animals; D001413:Bacillus thuringiensis; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism* / Q000633:toxicity; D001427:Bacterial Toxins / Q000378:metabolism* / Q000633:toxicity; D001665:Binding Sites; D004064:Digestive System / Q000201:enzymology / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D004731:Endotoxins / Q000378:metabolism* / Q000633:toxicity; D006460:Hemolysin Proteins; D007305:Insecticide Resistance; D007814:Larva / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism; D009036:Moths / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D010572:Pest Control, Biological; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012641:Selection, Genetic
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011956:Receptors, Cell Surface; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D010450:Endopeptidases