Monoclonal Antibody Analysis and Insecticidal Spectrum of Three Types of Lepidopteran-Specific Insecticidal Crystal Proteins of Bacillus thuringiensis

摘要: We have investigated the protein composition and insecticidal spectrum of crystals 29 Bacillus thuringiensis strains active against lepidopteran larvae. All contained proteins 130 to 140 kilodaltons (kDa) which could be grouped into three types by molecular weight protoxin trypsin-activated core fragment. Proteins showed a characteristic when tested five species. Type A crystal were protoxins or 133 kDa, processed 60-kDa toxins trypsin. Several genes encoding this type been cloned sequenced earlier. They are highly conserved in N-terminal half toxic fragment previously classified subtypes (the 4.5-, 5.3-, 6.6-kilobase subtypes) based on restriction map their genes. The present study shows that different these equally Manduca sexta Pieris brassicae had no detectable activity Spodoptera littoralis. However, differed toxicity Heliothis virescens Mamestra brassicae. B consisted 140-kDa with 55-kDa tryptic These only one insect species (P. brassicae). toxin C 135- 63-kDa proteins, respectively. associated high S. littoralis M. panel 35 monoclonal antibodies was used compare structural characteristics subtypes. Each typical epitope structure, indicating an unambiguous correlation between antigenic structure specificity.