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Updated: Jun 19, 2026

Following Cell-fate in E. coli After Infection by Phage Lambda
Published on: October 14, 2011
Complete genome sequence of a newly isolated lytic bacteriophage, EFAP-1 of Enterococcus faecalis, and antibacterial
1Laboratory of Animal Cell Biotechnology, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
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.
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