Comparative biochemistry of entomocidal parasporal crystals of selected Bacillus thuringiensis strains.
Parasporal crystals of Bacillus thuringiensis subspp. kurstaki, tolworthi, alesti, berliner, and israelensis were compared by electron microscopy, polyacrylamide gel electrophoresis, amino acid analysis, tryptic peptide mapping, immunological analysis, and insecticidal activity. Spore coats also were compared by polyacrylamide gel electrophoresis. B. thuringiensis subsp. israelensis crystals were lethally toxic to mosquito larvae and nontoxic to tobacco hornworm larvae. Conversely, crystals from the other subspecies killed tobacco hornworm larvae but were ineffective against mosquitoes. Crystalline inclusion bodies of all subspecies contained a protoxic subunit that had an apparent molecular weight of approximately 1.34 X 10(5). However, polyacrylamide gel electrophoretic patterns of solubilized crystals revealed a small-molecular-weight component (apparent molecular weight, 26,000) in B. thuringiensis subsp. israelensis that was absent in the other subspecies. Also, differences were noted in amino acid composition and tryptic peptide fingerprints. Crystal proteins were found in spore coats of all subspecies. The results suggest that insecticidal specificity is due to unique polypeptide toxins.
D000596:Amino Acids / Q000032:analysis; D001413:Bacillus thuringiensis / Q000032:analysis*; D001426:Bacterial Proteins / Q000032:analysis; D001427:Bacterial Toxins / Q000032:analysis* / Q000494:pharmacology; D002241:Carbohydrates / Q000032:analysis; D003461:Crystallography; D004175:Diptera / Q000187:drug effects; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis; D007915:Lepidoptera / Q000187:drug effects; D013045:Species Specificity; D013171:Spores, Bacterial / Q000032:analysis
D000596:Amino Acids; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D002241:Carbohydrates; D006023:Glycoproteins