Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b

FEMS Microbiol Lett. 1989 Jan 15;48(2):197-202. doi: 10.1111/j.1574-6968.1989.tb03298.x.

Abstract

In culture supernatants of both Listeria ivanovii and Listeria monocytogenes Sv4b, for the first time a hemolysin of molecular weight 58 kDa was identified, which had all the characteristics of an SH-activated cytolysin, and which was therefore identified as listeriolysin O (LLO). In the case of L. ivanovii a second major supernatant protein of molecular weight 24 kDa co-purified with LLO. However, the function of this protein has to be determined. In culture supernatants of L. ivanovii a sphingomyelinase and a lecithinase activity could be detected, both enzymatic activities together contributing to the pronounced hemolysis caused by L. ivanovii. The N-terminal amino acid sequences of LLO and the 24 kDa from L. ivanovii are shown.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins*
  • Heat-Shock Proteins / isolation & purification
  • Hemolysin Proteins / biosynthesis*
  • Hemolysin Proteins / isolation & purification
  • Hemolysin Proteins / physiology
  • Listeria / immunology*
  • Listeria / pathogenicity
  • Listeria monocytogenes / immunology
  • Listeria monocytogenes / pathogenicity
  • Molecular Sequence Data
  • Molecular Weight
  • Virulence

Substances

  • Bacterial Toxins
  • Heat-Shock Proteins
  • Hemolysin Proteins
  • hlyA protein, Listeria monocytogenes