Abstract
The crystal-forming proteins (δ-endotoxins) produced by various serotypes of Bacillus thuringiensis and toxic for Lepidoptera reveal the same pattern of molecular organisation. These proteins (M r of ca. 145,000–130,000) contain an N-terminal domain (M r of 85,000–65,000) resistant to proteolysis whereas their C-terminal moieties (M r of 65,000) undergo an extensive degradation by trypsin that leads to stepwise cleavage off the fragments with M r of 15,000–35,000.
The N-terminal domain from serotype V δ-endotoxin is active when introduced into the hemocoel of Galleria mellonella larvae. Hence, it correponds to the “true toxin” normally formed by larva proteases action on the crystalforming protein (protoxin). Some differences were found in the properties of the N-terminal domains isolated from the crystal-forming proteins of III, V and IX serotypes, e.g., in their solubility, digestion by subtilisin, molecular weights and the distribution of methionine residues along the polypeptide chains.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- SDS:
-
sodium dodecyl sulphate
- PAGE:
-
polyacryl amide gel electrophoresis
- CFP:
-
crystal-forming protein
- DNS:
-
5-dimethylamino-1-naphthalene-sulphonyl
References
Bulla LA, Jr, Kramer KJ, Cox DJ, Jones BL, Davidson I, Lookhart CL, (1981) Purification and characterization of the entomocidal protoxin of B. thuringiensis. J Biol Chem 256:3000–3004
Chestukhina GG, Kostina LI, Zalunin IA, Kotova TS, Katrukha SP, Kuznetsov YuS, Stepanov VM (1977) Proteins of B. thuringiensis crystals δ-endotoxin. Biokhimiya 42:1660–1667
Chestukhina GG, Zalunin IA, Kostina LI, Kotova TS, Katrukha SP, Lublinskaya LA, Stepanov VM (1978) Proteolytic enzymes bound to B. thuringiensis crystals. Biokhimiya 43:857–864
Chestukhina GG, Kotova TS, Zalunin IA, Stepanov VM (1979) Proteinases in growth and spore formation of B. thuringiensis. Biokhimiya 44:796–802
Chestukhina GG, Zalunin IA, Kostina LI, Kotova TS, Katrukha SP, Stepanov VM (1980) Crystal-forming proteins of B. thuringiensis. Limited proteolysis by endogenous proteinases as a cause of their apparent multiplicity. Biochem J 187:457–465
Huber HE, Lüthy P, Ebersold H-R, Cordier J-L (1981) The subunits of the parasporal crystal of B. thuringiensis: size, linkage and toxicity. Arch Microbiol 129:14–18
Lecadet MM, Martouret D (1962) La toxine figure de B. thuringiensis: Production enzymatique de substances solubles toxiques par injection. C R Acad Sci 254:2457–2459
Lilley M, Ruffell RN, Somerville HJ (1980) Purification of the insecticidal toxin in crystal of B. thuringiensis. J Gen Microbiol 118:1–12
Spencer IJ (1968) Comparative amino acid compositions of the parasporal inclusions of five entomopathogeneous bacteria. J Inverteb Pathol 10:444–445
Stepanov VM, Chestukhina GG, Rudenskaya GN, Epremyan AS, Osterman AL, Khodova OM, Belyanova LP (1981) A new subfamily of microbial proteinases? Structural similarities of B. thuringiensis and Thermoactinomyces vulgaris extracellular serine proteinases. Biochem Biophys Res Commun 100:1680–1687
Tyrell DJ, Bulla LA Jr, Andrews RE Jr, Kramer KJ, Davidson LI, Nordin PH (1981) Comparative biochemistry of entomocidal parasporal crystals of selected B. thuringiensis strains. J Bacteriol 145:1052–1062
Weber K, Osborn M (1969) The reliability of molecular weight determinations by dodecyl sulfate polyacrylamide gel electrophoresis. J Biol Chem 244:4406–4412
Zalunin IA, Chestukhina GG, Stepanov VM (1979) Protein composition of δ-endotoxin crystals in various serotypes of B. thuringiensis. Biokhimiya 44:639–698
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Chestukhina, G.G., Kostina, L.I., Mikhailova, A.L. et al. The main features of Bacillus thuringiensis δ-endotoxin molecular structure. Arch. Microbiol. 132, 159–162 (1982). https://doi.org/10.1007/BF00508723
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00508723