| Literature DB >> 26896930 |
Pengjuan Gong1, Mengjun Cheng1, Xinwei Li1, Haiyan Jiang2, Chuang Yu1, Nadire Kahaer1, Juecheng Li1, Lei Zhang1, Feifei Xia1, Liyuan Hu1, Changjiang Sun1, Xin Feng1, Liancheng Lei1, Wenyu Han3, Jingmin Gu4.
Abstract
Due to the worldwide prevalence of antibiotic resistant strains, phages therapy has been revitalized recently. In this study, an Enterococcus faecium phage named IME-EFm5 was isolated from hospital sewage. Whole genomic sequence analysis demonstrated that IME-EFm5 belong to the Siphoviridae family, and has a double-stranded genome of 42,265bp (with a 35.51% G+C content) which contains 70 putative coding sequences. LysEFm5, the endolysin of IME-EFm5, contains an amidase domain in its N-terminal and has a wider bactericidal spectrum than its parental phage IME-EFm5, including 7 strains of vancomycin-resistant E. faecium. The mutagenesis analysis revealed that the zinc ion binding residues (H27, H132, and C140), E90, and T138 are required for the catalysis of LysEFm5. However, the antibacterial activity of LysEFm5 is zinc ion independent, which is inconsistent with most of other amidase members. The phage lysin LysEFm5 might be an alternative treatment strategy for infections caused by multidrug-resistant E. faecium.Entities:
Keywords: Amidase; Enterococcus faecium; Phage lysin; Zinc-dependent
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Year: 2016 PMID： 26896930 DOI： 10.1016/j.virol.2016.02.006
Source DB: PubMed Journal: Virology ISSN： 0042-6822 Impact factor: 3.616