Proteinase-mediated insect resistance to Bacillus thuringiensis toxins.
Two Bacillus thuringiensis (Bt)-resistant strains of the Indianmeal moth, Plodia interpunctella, lack a major gut proteinase that activates Bt protoxins. The absence of this enzyme is genetically linked to larval survival on Bt-treated diets. When considered with previous data supporting the existence of receptor-mediated insect resistance to Bt, these results provide evidence that insect adaptation to these toxins occurs through multiple physiological mechanisms, which complicate efforts to prevent or manage resistance to Bt toxins in insect control programs.
Oppert
B
B
United States Grain Marketing Research Laboratory, United States Department of Agriculture, Agricultural Research Service, Manhattan, Kansas 66502-2736, USA. bso@ksu.edu
Kramer
K J
KJ
Beeman
R W
RW
Johnson
D
D
McGaughey
W H
WH
D000818:Animals; D001413:Bacillus thuringiensis / Q000737:chemistry*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000633:toxicity*; D001427:Bacterial Toxins; D004731:Endotoxins / Q000633:toxicity*; D005260:Female; D006460:Hemolysin Proteins; D006868:Hydrolysis; D007422:Intestines / Q000201:enzymology; D007814:Larva / Q000187:drug effects / Q000201:enzymology; D008297:Male; D009036:Moths / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D010572:Pest Control, Biological; D012697:Serine Endopeptidases / Q000378:metabolism*
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D012697:Serine Endopeptidases