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

Cecilia Martini, Charlotte Michaux, Francesca Bugli, Alessandro Arcovito, Federica Iavarone, Margherita Cacaci, Francesco Paroni Sterbini, Axel Hartke, Nicolas Sauvageot, Maurizio Sanguinetti, Brunella Posteraro, Jean-Christophe Giard

Risultato della ricerca: Contributo in rivistaArticolo in rivista

4 Citazioni (Scopus)


We previously showed that the mutant strain of Enterococcus faecalis lacking the transcriptional regulator SlyA is more virulent than the parental strain. We hypothesized that this phenotype was due to overexpression of the second gene of the slyA operon, ef_3001, renamed pmvE (for polyamine metabolism and virulence of E. faecalis). PmvE shares strong homologies with N(1)-spermidine/spermine acetyltransferase enzymes involved in the metabolism of polyamines. In this study, we used an E. faecalis strain carrying the recombinant plasmid pMSP3535-pmvE (V19/p3535-pmvE), which allows the induction of pmvE by addition of nisin. Thereby, we showed that the overexpression of PmvE increased the virulence of E. faecalis in the Galleria mellonella infection model, as well as the persistence within peritoneal macrophages. We were also able to show a direct interaction between the His-tagged recombinant PmvE (rPmvE) protein and putrescine by the surface plasmon resonance (SPR) technique on a Biacore instrument. Moreover, biochemical assays showed that PmvE possesses an N-acetyltransferase activity toward polyamine substrates. Our results suggest that PmvE contributes to the virulence of E. faecalis, likely through its involvement in the polyamine metabolism.
Lingua originaleEnglish
pagine (da-a)364-371
Numero di pagine8
RivistaInfection and Immunity
Stato di pubblicazionePubblicato - 2015


  • Acetyltransferases
  • Animals
  • Enterococcus faecalis
  • Gene Expression
  • Lepidoptera
  • Protein Binding
  • Putrescine
  • Surface Plasmon Resonance
  • Virulence


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