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Autor:
Xiaoping Xu, David McCaskill, Vimbai M. Chikwana, Sek Yee Tan, Thimothy Hey, Eva Fortea, Léna Potvin, Jean-Louis Schwartz, Vincent Vachon, Vincent Lemieux, Samantha Griffin, Kenneth E. Narva
Publikováno v:
Journal of Biological Chemistry. 292:13122-13132
Cry6Aa1 is a Bacillus thuringiensis (Bt) toxin active against nematodes and corn rootworm insects. Its 3D molecular structure, which has been recently elucidated, is unique among those known for other Bt toxins. Typical three-domain Bt toxins permeab
Autor:
Monique Royer, Roger Frutos, Roland Brousseau, Jean-Louis Schwartz, Sébastien Rivest, Florence Coux, Luke Masson, Kouros Moozar, Cécile Rang, Raynald Laprade, Vincent Vachon, Martine Bes
Publikováno v:
Journal of Biological Chemistry
The four salt bridges (Asp(222)-Arg(281), Arg(233)-Glu(288), Arg(234)-Glu(274), and Asp(242)-Arg(265)) linking domains I and II in Cry1Aa were abolished individually in alpha-helix 7 mutants D222A, R233A, R234A, and D242A. Two additional mutants targ
Publikováno v:
Journal of Biological Chemistry. 271:25220-25226
Alanine substitutions of loop 3 residues, 438SGFSNS443, of CryIAb toxin were constructed to study the functional role of these residues in receptor binding and toxicity to Manduca sexta and Heliothis virescens. Experiments with trypsin and insect gut
Publikováno v:
Journal of Biological Chemistry. 277:23985-23987
A variant form of the Bacillus thuringiensis Cry1Ac toxin that is not cleaved at the N terminus during proteolytic activation with trypsin was found to be incapable of forming pores in Manduca sexta brush border membrane vesicles in vitro and had red