Involvement of peptidylprolyl cis/trans isomerases in Enterococcus faecalis virulence

Maurizio Sanguinetti, Brunella Posteraro, Fany Reffuveille, Nathalie Connil, Sylvie Chevalier, Yanick Auffray, Alain Rince

Risultato della ricerca: Contributo in rivistaArticolo in rivistapeer review

22 Citazioni (Scopus)

Abstract

Peptidylprolyl cis/trans isomerases (PPIases) are enzymes involved in protein folding. Analysis of the genome sequence of Enterococcus faecalis V583 allowed for identification of 3 PPIases carrying genes. ef2898 encodes an intracellular PPIase which was not shown to be important for the E. faecalis stress response or virulence. The other two PPIases, the parvulin family rotamase EF0685 and the cyclophilin family member EF1534, are expected to be surface-exposed proteins. They were shown to be important for virulence and resistance to NaCl. A Δef0685 Δef1534 mutant was also more resistant to oxidative stress, was able to grow under a high manganese concentration, and showed altered resistance to ampicillin and quinolone antibiotics.
Lingua originaleEnglish
pagine (da-a)1728-1735
Numero di pagine8
RivistaInfection and Immunity
Volume80
DOI
Stato di pubblicazionePubblicato - 2012

Keywords

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins
  • Enterococcus faecalis
  • Female
  • Gene Expression Regulation, Bacterial
  • Gene Expression Regulation, Enzymologic
  • Genetic Complementation Test
  • Gram-Positive Bacterial Infections
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Mutation
  • Peptidylprolyl Isomerase
  • Virulence

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