Specificity of Bacillus thuringiensis delta-endotoxins is correlated with the presence of high-affinity binding sites in the brush border membrane of target insect midguts.

@article{Hofmann1988SpecificityOB,
  title={Specificity of Bacillus thuringiensis delta-endotoxins is correlated with the presence of high-affinity binding sites in the brush border membrane of target insect midguts.},
  author={Christina Hofmann and H Vanderbruggen and Herman H{\"o}fte and Jeroen Van Rie and Stefan Jansens and H Van Mellaert},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1988},
  volume={85 21},
  pages={7844-8}
}
Binding studies were performed with two 125I-labeled Bacillus thuringiensis delta-endotoxins on brush border membrane vesicles prepared from the larval midgut of the tobacco hornworm Manduca sexta or the cabbage butterfly Pieris brassicae. One delta-endotoxin, Bt2-protoxin, is a 130-kDa recombinant crystalline protein from B. thuringiensis subsp. berliner. It kills larvae of both insect species. The active Bt2-toxin is a 60-kDa proteolytic fragment of the Bt2-protoxin. It binds saturably and… CONTINUE READING
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