Bacillus thuringiensis ssp. galleriae simultaneously produces two δ-endotoxins differing strongly in primary structure and entomocidal activity

AbstractStrain 11–67 of B. thuringiensis ssp. galleriae produces two entomocidal proteins of molecular mass 130 kDa. Limited proteolysis of these proteins — protoxins — yields the ‘true’ toxins of molecular mass 65 kDa which are drastically different with respect to their charges at pH 8.6, immunological properties and toxicity (host range). One of the proteins — the ‘negative’ component — is toxic for Lymantria dispar larvae and shows 65% homology when compared with B. thuringiensis ssp. kurstaki δ-endotoxins. The other — the ‘positive’ component — is toxic for Galleria mellonella larvae. Its N-terminal sequence of 11 amino acid residues is homologous with the B. thuringiensis ssp. israelensis and san diego endotoxins known to be toxic for Coleoptera and Diptera but not for Lepidoptera. Hence, B. thuringiensis subspecies may produce simultaneously δ-endotoxins differing substantially in structural features and host range

Study of Structure and Functions of Delta-Endotoxins and Proteinases Bac. thuringiensis (Scientific Report)

Available from VNTIC / VNTIC - Scientific & Technical Information Centre of RussiaSIGLERURussian Federatio