Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes

Arch Microbiol. 1985 Apr;141(3):249-54. doi: 10.1007/BF00408067.

Abstract

Pep 5 and nisin are cationic bactericidal peptides which were shown to induce autolysis in Staphylococcus cohnii 22. In contrast to nisin, Pep 5 induced lysis could be stimulated in the presence of glucose. Addition of lipoteichoic acids (LTA) (D-alanine:phosphorus = 0.475:1) inhibited all effects of Pep 5 on susceptible cells in a molar ratio LTA:Pep 5 of 10:1. Treatment of S. cohnii 22 with Pep 5 or nisin for 20 min and subsequent washing with 2.5 M NaCl released autolysin activity. Crude preparations of the hydrolyzing enzymes produced free amino groups as well as polysaccharide fragments from the murein backbone, suggesting the presence of a muramidase or glucosamidase, and endopeptidase or amidase. Both enzyme activities were inhibited by lipoteichoic acid; they could be fully reactivated by addition of Pep 5 in sufficient concentrations. The velocity of hydrolysis was not influenced by nisin, whereas it was doubled in presence of Pep 5. The results are discussed in view of a possible mechanism of induction of lysis by Pep 5 and nisin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacteriocins / pharmacology*
  • Bacteriolysis / drug effects*
  • Lipopolysaccharides*
  • Nisin / pharmacology*
  • Peptides / pharmacology
  • Phosphatidic Acids / pharmacology
  • Staphylococcus / drug effects*
  • Staphylococcus / enzymology
  • Teichoic Acids / pharmacology

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • Lipopolysaccharides
  • Peptides
  • Phosphatidic Acids
  • Teichoic Acids
  • Nisin
  • staphylococcin
  • lipoteichoic acid