Enterococcal quorum-controlled protease alters phage infection.

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.