A novel bacteriocin from Enterococcus faecalis 478 exhibits a potent activity against vancomycin-resistant enterococci

PLoS One. 2017 Oct 12;12(10):e0186415. doi: 10.1371/journal.pone.0186415. eCollection 2017.

Abstract

The emergence of multidrug-resistant enterococci (MDRE) and particularly vancomycin-resistant enterococci (VRE) is considered a serious health problem worldwide, causing the need for new antimicrobials. The aim of this study was to discover and characterize bacteriocin against clinical isolates of MDRE and VRE. Over 10,000 bacterial isolates from water, environment and clinical samples were screened. E. faecalis strain 478 isolated from human feces produced the highest antibacterial activity against several MDRE and VRE strains. The optimum condition for bacteriocin production was cultivation in MRS broth at 37°C, pH 5-6 for 16 hours. The bacteriocin-like substance produced from E. faecalis strain EF478 was stable at 60°C for at least 1 hour and retained its antimicrobial activity after storage at -20°C for 1 year, at 4°C for 6 months, and at 25°C for 2 months. A nano-HPLC electrospray ionization multi-stage tandem mass spectrometry (nLC-ESI-MS/MS) analysis showed that the amino acid sequences of the bacteriocin-like substance was similar to serine protease of E. faecalis, gi|488296663 (NCBI database), which has never been reported as a bacteriocin. This study reported a novel bacteriocin with high antibacterial activity against VRE and MDRE.

MeSH terms

  • Amino Acid Sequence
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / isolation & purification
  • Anti-Infective Agents / pharmacology*
  • Bacteriocins / chemistry*
  • Bacteriocins / isolation & purification
  • Bacteriocins / pharmacology
  • DNA / chemistry
  • DNA / isolation & purification
  • DNA / metabolism
  • Enterococcus faecalis / isolation & purification
  • Enterococcus faecalis / metabolism*
  • Feces / microbiology
  • Humans
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Nanotechnology
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Serine Proteases / chemistry
  • Spectrometry, Mass, Electrospray Ionization
  • Temperature
  • Vancomycin-Resistant Enterococci / drug effects*

Substances

  • Anti-Infective Agents
  • Bacteriocins
  • DNA
  • Serine Proteases

Grants and funding

The study was partially supported for publication by the China Medical Board (CMB), Faculty of Public Health, Mahidol University, Bangkok, Thailand. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.