Induction of autolysis in Enterococcus faecalis S-47 by peptide AS-48

J Appl Bacteriol. 1990 Sep;69(3):406-13. doi: 10.1111/j.1365-2672.1990.tb01531.x.

Abstract

In addition to its bactericidal mode of action, the peptide antibiotic AS-48 exhibits a bacteriolytic effect on Enterococcus faecalis S-47 that is associated with autolysin activation. Bacteriolysis induced by the antibiotic can be modulated by addition of EDTA, divalent cations and autolysin activators (trypsin) or inhibitors (cardiolipin), suggesting that topologic regulation of the autolysins is involved in the process. In addition, inhibitors of protein and RNA synthesis interfere markedly with bacteriolysis, as do ionophores and the ATPase inhibitor DCCD, suggesting the participation of an internal messenger in autolysin activation in the presence of AS-48.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents* / pharmacology*
  • Bacterial Proteins / biosynthesis
  • Bacteriolysis / drug effects*
  • Cardiolipins / pharmacology
  • Cations, Divalent / pharmacology
  • Dicyclohexylcarbodiimide / pharmacology
  • Edetic Acid / pharmacology
  • Enterococcus faecalis / drug effects*
  • Enterococcus faecalis / genetics
  • Enterococcus faecalis / metabolism
  • Gramicidin / pharmacology
  • Humans
  • Membrane Potentials
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism*
  • Peptides / pharmacology
  • RNA, Bacterial / biosynthesis
  • Sodium Dodecyl Sulfate / pharmacology
  • Temperature
  • Trypsin / pharmacology

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Cardiolipins
  • Cations, Divalent
  • Peptides
  • RNA, Bacterial
  • BacA protein, Enterococcus faecalis
  • Gramicidin
  • Sodium Dodecyl Sulfate
  • Dicyclohexylcarbodiimide
  • Edetic Acid
  • Trypsin
  • N-Acetylmuramoyl-L-alanine Amidase