Effect of removal of the cytolytic factor of Bacillus thuringiensis subsp. israelensis on mosquito toxicity.
Solubilized crystal protein of Bacillus thuringiensis subsp. israelensis was fractionated by affinity chromatography using a monoclonal antibody directed against the crystal's 28 kDa peptide. The 28 kDa peptide was found to be relatively nontoxic to mosquito larvae although it does contain the hemolytic activity of the crystals. The crystal protein fraction depleted of the 28 kDa peptide was found to be nonhemolytic and to retain nearly full toxicity to mosquito larvae. These results suggest that the 28 kDa peptide is not required for the toxicity of solubilized crystal protein.
D000330:Aedes / Q000187:drug effects*; D000818:Animals; D000911:Antibodies, Monoclonal; D001413:Bacillus thuringiensis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D002846:Chromatography, Affinity; D003460:Crystallization; D007159:Immunologic Tests; D007814:Larva / Q000187:drug effects; D008970:Molecular Weight; D012995:Solubility
D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins