Complete genome sequence of a newly isolated lytic bacteriophage, EFAP-1 of Enterococcus faecalis, and antibacterial activity of its endolysin EFAL-1

J Appl Microbiol. 2010 May;108(5):1769-79. doi: 10.1111/j.1365-2672.2009.04576.x. Epub 2009 Oct 7.

Abstract

Aims: In this work, we aimed to identify an effective treatment of infections caused by Enterococcus spp. strains resistant to conventional antibiotics.

Methods and results: We report the isolation and characterization of a new lytic bacteriophage, designated bacteriophage EFAP-1, that is capable of lysing Enterococcus faecalis bacteria that exhibit resistance to multiple antibiotics. EFAP-1 has low sequence similarity to all known bacteriophages. Transmission electron microscopy confirmed that EFAP-1 belongs to the Siphoviridae family. A putative lytic protein of EFAP-1, endolysin EFAL-1, is encoded in ORF 2 and was expressed in Escherichia coli. Recombinant EFAL-1 had broad-spectrum lytic activity against several Gram-positive pathogens, including Ent. faecalis and Enterococcus faecium.

Conclusions: The complete genome sequence of the newly isolated enterococcal lytic phage was analysed, and it was demonstrated that its recombinant endolysin had broad lytic activity against various Gram-positive pathogens.

Significance and impact of the study: Bacteriophage EFAP-1 and its lytic protein, EFAL-1, can be utilized as potent antimicrobial agents against Enterococcus spp. strains resistant to conventional antibiotics in hospital infections and also as environmental disinfectants to control disease-causing Enterococcus spp. in dairy farms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacteriophages / classification
  • Bacteriophages / genetics*
  • Bacteriophages / isolation & purification
  • Bacteriophages / ultrastructure
  • Endopeptidases / genetics
  • Endopeptidases / isolation & purification
  • Endopeptidases / pharmacology*
  • Enterococcus faecalis / drug effects
  • Enterococcus faecalis / virology*
  • Genome, Viral*
  • Gram-Positive Bacteria / drug effects*
  • Molecular Sequence Data
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / pharmacology
  • Siphoviridae / classification
  • Siphoviridae / genetics
  • Siphoviridae / isolation & purification
  • Siphoviridae / ultrastructure
  • Viral Proteins / genetics
  • Viral Proteins / isolation & purification
  • Viral Proteins / pharmacology

Substances

  • Anti-Bacterial Agents
  • Recombinant Proteins
  • Viral Proteins
  • Endopeptidases
  • endolysin

Associated data

  • GENBANK/FJ792813