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PMID: 7085565 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Relationship of the syntheses of spore coat protein and parasporal crystal protein in Bacillus thuringiensis.

Journal of bacteriology ·Vol. 151 ·No. 1 ·1982-07-00 ·Pages 399-410

Aronson AI, Tyrell DJ, Fitz-James PC, Bulla LA

Abstract

Two major classes of polypeptides were extracted from the spore surface of Bacillus thuringiensis subsp. kurstaki: the 134,000-dalton protoxin that is the major component of the crystalline inclusion and spore coat polypeptides very similar to those found on Bacillus cereus spores. The quantity of spore coat polypeptides produced was reduced when compared with that produced by certain acrystalliferous mutants or by B. thuringiensis subsp. israelensis. The latter organism produced an inclusion toxic to mosquito larvae, but deposited very little of the inclusion protein on the spore surface. The reduction in spore coat protein in B. thuringiensis subsp. kurstaki was also seen in freeze-etched electron micrographs of spores. B. thuringiensis subsp. kurstaki spores germinated rather slowly when compared with related species, a property previously correlated with a deficiency or defect of the spore coat. Many mutants of B. thuringiensis subsp. kurstaki unable to form a crystalline inclusion were nontoxic and lacked a well-defined spore coat. Other mutants isolated either directly from the wild type or from coat-deficient mutants produced spores that were identical to those produced by the closely related species. Bacillus cereus, on the basis of morphology, germination rate, and the size and antigenicity of the spore coat polypeptides. Most of the protein extractable from the inclusion produced by B. thuringiensis subsp. israelensis was about 26,000 daltons, considerably smaller than the major polypeptide extractable from other inclusions. Some of the B. thuringiensis subsp. israelensis inclusion protein was found on the spore surface, but the majority of the extractable spore coat protein was the same size and antigenicity as that found on B. cereus spores. The B. thuringiensis subsp. israelensis spores germinated at a rate close to that of B. cereus, especially when the spores were formed at 37 degrees C, and the morphology of the spore surface was very similar to that of B. cereus.

MeSH Terms
Bacillus thuringiensis/metabolism,ultrastructure Bacterial Proteins/biosynthesis,isolation & purification Cell Membrane/metabolism,ultrastructure Electrophoresis, Polyacrylamide Gel Freeze Etching Kinetics Microscopy, Electron Spores, Bacterial/metabolism,ultrastructure
Chemicals
Bacterial Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Aronson A I
Tyrell D J
Fitz-James P C
Bulla L A
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1982-07-00
Pages
399-410
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC220252
Subset
IM
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