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

다국어 초록 (Multilingual Abstract)

<P>Abstract</P><P>Aims: </P><P>In this work, we aimed to identify an effective treatment of infections caused by <I>Enterococcus</I> spp. strains resistant to conventional antibiotics.</P><P>Methods and Results: </P><P>We report the isolation and characterization of a new lytic bacteriophage, designated bacteriophage EFAP-1, that is capable of lysing <I>Enterococcus faecalis</I> 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 <I>Siphoviridae</I> family. A putative lytic protein of EFAP-1, endolysin EFAL-1, is encoded in ORF 2 and was expressed in <I>Escherichia coli</I>. Recombinant EFAL-1 had broad-spectrum lytic activity against several Gram-positive pathogens, including <I>Ent. faecalis</I> and <I>Enterococcus faecium.</I></P><P>Conclusions: </P><P>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.</P><P>Significance and Impact of the Study: </P><P>Bacteriophage EFAP-1 and its lytic protein, EFAL-1, can be utilized as potent antimicrobial agents against <I>Enterococcus</I> spp. strains resistant to conventional antibiotics in hospital infections and also as environmental disinfectants to control disease-causing <I>Enterococcus</I> spp. in dairy farms.</P>