The toxicity of two Bacillus thuringiensis delta-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxins.
The delta-endotoxin from Bacillus thuringiensis subspecies kurstaki strain HD1-9 is almost 400 times more potent than the delta-endotoxin from strain HD-73 as a gypsy moth larvicide. The two delta-endotoxins compete for a high-affinity binding site on the brush border membrane of larval gypsy moth midguts. The affinity for the delta-endotoxin from strain HD-73 is much greater than the affinity for the delta-endotoxin from strain HD1-9.
Wolfersberger
M G
MG
Department of Biology, Temple University, Philadelphia, Pennsylvania 19122.
D000818:Animals; D001413:Bacillus thuringiensis; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D001665:Binding Sites; D004731:Endotoxins / Q000378:metabolism / Q000633:toxicity*; D005753:Gastric Mucosa / Q000378:metabolism*; D006460:Hemolysin Proteins; D007306:Insecticides / Q000378:metabolism / Q000633:toxicity*; D007814:Larva; D007915:Lepidoptera / Q000378:metabolism*; D008871:Microvilli / Q000378:metabolism; D009036:Moths / Q000378:metabolism*; D013270:Stomach / Q000648:ultrastructure
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D007306:Insecticides; C030956:insecticidal crystal protein, Bacillus Thuringiensis