Complete genome sequence of a newly isolated lytic bacteriophage, EFAP-1 of Enterococcus faecalis, and antibacterial activity of its endolysin EFAL-1.
OBJECTIVE
In this work, we aimed to identify an effective treatment of infections caused by Enterococcus spp. strains resistant to conventional antibiotics.


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.


CONCLUSIONS
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.
Laboratory of Animal Cell Biotechnology, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
J S
JS
Son
S Y
SY
Jun
E B
EB
Kim
J E
JE
Park
H R
HR
Paik
S J
SJ
Yoon
S H
SH
Kang
Y-J
YJ
Choi
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001435:Bacteriophages / Q000145:classification / Q000235:genetics* / Q000302:isolation & purification / Q000648:ultrastructure; D010450:Endopeptidases / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D013293:Enterococcus faecalis / Q000187:drug effects / Q000821:virology*; D016679:Genome, Viral; D006094:Gram-Positive Bacteria / Q000187:drug effects*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology; D017906:Siphoviridae / Q000145:classification / Q000235:genetics / Q000302:isolation & purification / Q000648:ultrastructure; D014764:Viral Proteins / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D011994:Recombinant Proteins; D014764:Viral Proteins; D010450:Endopeptidases; C001143:endolysin