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Enterococcal quorum-controlled protease alters phage infection.

Emma K Sheriff1, Fernanda Salvato2, Shelby E Andersen1

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Bacteriophages (phages) show promise against resistant bacteria. This study reveals how phage VPE25 impacts Enterococcus faecalis, identifying bacterial protein changes and a key virulence factor, GelE, that influences phage infection.

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Area of Science:

  • Microbiology
  • Bacteriophage Therapy
  • Proteomics

Background:

  • Rising multidrug-resistant bacterial infections necessitate novel antimicrobials like bacteriophages (phages).
  • Understanding phage-host interactions is crucial for optimizing phage therapy effectiveness.
  • Enterococcus faecalis infections pose a significant public health challenge.

Approach:

  • Proteomic analysis was conducted on Enterococcus faecalis during infection with bacteriophage VPE25.
  • Bacterial protein abundance changes were quantified, with a focus on enterococcal gelatinase (GelE).
  • Plaque assays were performed on mutant strains (fsrA, gelE) to assess phage infection dynamics.

Key Points:

  • Numerous uncharacterized phage proteins were identified during E. faecalis infection.
  • Hundreds of bacterial protein abundance changes were observed, including a reduction in GelE.
  • GelE and its regulators (LrgA, LrgB) play a role in phage resistance, with mutations leading to increased plaque size.

Conclusions:

  • Phage VPE25 infection alters E. faecalis proteome, reducing virulence factors like GelE.
  • GelE-mediated protection against phage infection is linked to LrgA and LrgB.
  • Modulating GelE production could be a strategy to enhance phage therapy efficacy against E. faecalis.