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The polyamine N-acetyltransferase-like enzyme PmvE plays a role in the virulence of Enterococcus faecalis

Cecilia Martini1, Charlotte Michaux2, Francesca Bugli3

  • 1Equipe Stress Virulence, Unité de Recherche Risques Microbiens (U2RM), Université de Caen, Caen, France Institute of Microbiology, Catholic University of Sacred Heart, Rome, Italy.

Infection and Immunity
|November 12, 2014
PubMed

Insights

A key virulence factor in Enterococcus faecalis, PmvE, contributes to bacterial infection and persistence. This polyamine metabolism enzyme enhances pathogen virulence, offering new targets for therapeutic strategies.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Enterococcus faecalis virulence is linked to specific genetic factors.
  • The slyA operon and its gene ef_3001 (pmvE) were implicated in E. faecalis pathogenicity.

Purpose of the Study:

  • To investigate the role of PmvE in Enterococcus faecalis virulence.
  • To characterize the enzymatic activity and interactions of PmvE.

Main Methods:

  • Overexpression of pmvE in E. faecalis using a nisin-inducible plasmid.
  • Galleria mellonella infection model to assess virulence.
  • Macrophage persistence assays.
  • Surface Plasmon Resonance (SPR) for protein-ligand interaction analysis.
  • Biochemical assays for N-acetyltransferase activity.

Main Results:

  • Overexpression of PmvE significantly increased E. faecalis virulence in G. mellonella.
  • PmvE enhanced bacterial persistence within peritoneal macrophages.
  • Direct binding of recombinant PmvE (rPmvE) to putrescine was confirmed via SPR.
  • Biochemical assays demonstrated PmvE's N-acetyltransferase activity on polyamine substrates.

Conclusions:

  • PmvE is a crucial virulence factor in E. faecalis.
  • PmvE's N-acetyltransferase activity in polyamine metabolism contributes to bacterial virulence and persistence.

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