Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes.
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.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001430:Bacteriocins / Q000494:pharmacology*; D001433:Bacteriolysis / Q000187:drug effects*; D008070:Lipopolysaccharides; D009561:Nisin / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology; D010712:Phosphatidic Acids / Q000494:pharmacology; D013210:Staphylococcus / Q000187:drug effects* / Q000201:enzymology; D013682:Teichoic Acids / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D008070:Lipopolysaccharides; D010455:Peptides; D010712:Phosphatidic Acids; D013682:Teichoic Acids; D009561:Nisin; C017724:staphylococcin; C009900:lipoteichoic acid