Sphingomyelinase is part of the 'enterotoxin complex' produced by Bacillus cereus

FEMS Microbiol Lett. 1993 Jun 1;110(1):97-100. doi: 10.1111/j.1574-6968.1993.tb06301.x.

Abstract

The three components of the 'enterotoxin complex' have been purified and the sequence of the first 14-15 amino acids of the proteins determined. Limited homology was found in the N-terminal sequence of the three proteins. The molecular mass of the proteins was determined to be 48, 40 and 34 kDa, respectively. Only the 40-kDa protein was toxic to Vero cells, whilst the 34-kDa protein was found to be hemolytic. The sequence of the first 14 N-terminal amino acids of this protein was identical to the sequence of the sphingomyelinase residues 28-41 (the N-terminal after loss of the signal sequence), except for a change from Gln to Glu in position 33 of the sphingomyelinase sequence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacillus cereus / enzymology*
  • Bacterial Proteins / chemistry
  • Bacterial Toxins / chemistry*
  • Enterotoxins / chemistry*
  • Molecular Sequence Data
  • Sphingomyelin Phosphodiesterase / chemistry*
  • Vero Cells

Substances

  • Bacterial Proteins
  • Bacterial Toxins
  • Enterotoxins
  • Sphingomyelin Phosphodiesterase

Associated data

  • SWISSPROT/P11889
  • SWISSPROT/P80172
  • SWISSPROT/P80173