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

A Gálvez1, E Valdivia, M Martínez-Bueno

  • 1Departamento de Microbiología, Facultad de Ciencias, Universidad de Granada, Spain.

The Journal of Applied Bacteriology
|September 1, 1990
PubMed

Insights

The peptide antibiotic AS-48 not only kills bacteria but also causes them to lyse by activating autolysins. This process involves internal messengers and is influenced by various chemical factors.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The peptide antibiotic AS-48 possesses known bactericidal properties.
  • Its potential to induce bacterial lysis requires further investigation.

Purpose of the Study:

  • To investigate the bacteriolytic effect of AS-48 on Enterococcus faecalis S-47.
  • To elucidate the mechanisms underlying AS-48-induced bacterial lysis, focusing on autolysin activation.

Main Methods:

  • Assessing the bacteriolytic effect of AS-48 on Enterococcus faecalis S-47.
  • Investigating the modulation of bacteriolysis by EDTA, divalent cations, and autolysin modulators (trypsin, cardiolipin).
  • Examining the impact of protein/RNA synthesis inhibitors, ionophores, and ATPase inhibitors (DCCD) on AS-48-induced bacteriolysis.

Main Results:

  • AS-48 induces bacteriolysis in Enterococcus faecalis S-47, linked to autolysin activation.
  • Bacteriolysis is modulated by EDTA, divalent cations, trypsin, and cardiolipin, indicating topologic regulation of autolysins.
  • Inhibitors of protein/RNA synthesis, ionophores, and DCCD significantly affect bacteriolysis, suggesting an internal messenger's role.

Conclusions:

  • AS-48-induced bacteriolysis in Enterococcus faecalis involves autolysin activation.
  • The process is regulated topographically and likely involves an internal messenger system.
  • These findings offer insights into the multifaceted action of peptide antibiotics.

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