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Updated: May 25, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Involvement of peptidylprolyl cis/trans isomerases in Enterococcus faecalis virulence
Fany Reffuveille1, Nathalie Connil, Maurizio Sanguinetti
1USC INRA 2017, Microbiologie de l'Environnement, EA956, Université de Caen, Caen, France.
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.
Insights
Three peptidylprolyl cis/trans isomerases (PPIases) were identified in Enterococcus faecalis. Two surface-exposed PPIases, EF0685 and EF1534, are crucial for virulence and resistance to environmental stressors.
Area of Science:
- Microbiology
- Molecular Biology
- Enzymology
Background:
- Peptidylprolyl cis/trans isomerases (PPIases) are critical enzymes facilitating protein folding.
- Enterococcus faecalis is a significant opportunistic pathogen.
- Understanding bacterial virulence factors is key to developing new therapeutic strategies.
Purpose of the Study:
- To identify and characterize PPIases in Enterococcus faecalis V583.
- To investigate the role of identified PPIases in bacterial virulence and stress response.
- To explore the potential of PPIases as targets for antimicrobial development.
Main Methods:
- Genome sequence analysis of Enterococcus faecalis V583 to identify PPIase genes.
- Gene knockout studies (Δef0685, Δef1534) to assess mutant phenotypes.
- Phenotypic analysis of wild-type and mutant strains under various stress conditions (NaCl, oxidative stress, manganese concentration, antibiotics).
Main Results:
- Three PPIase genes were identified in E. faecalis V583.
- The intracellular PPIase (ef2898) did not appear essential for virulence or stress response.
- Surface-exposed PPIases (EF0685 and EF1534) were vital for virulence and resistance to NaCl, oxidative stress, high manganese, ampicillin, and quinolones.
Conclusions:
- The parvulin family rotamase EF0685 and cyclophilin family member EF1534 are important virulence factors in E. faecalis.
- These surface-exposed PPIases contribute to bacterial survival under various environmental stresses.
- Targeting these PPIases could represent a novel approach to combat E. faecalis infections.
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