Characterization of Enterococcus faecium bacteriophage IME-EFm5 and its endolysin LysEFm5
Characterization of Enterococcus faecium bacteriophage IME-EFm5 and its endolysin LysEFm5
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屎肠球菌噬菌体 IME-EFm5 及其内溶素 LysEFm5 的表征
DOI：
10.1016/j.virol.2016.02.006
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发表时间：
2016-05-01
期刊：
影响因子：
3.7
通讯作者：
Gu, Jingmin
中科院分区：
文献类型：
--
作者：
Gong, Pengjuan;Cheng, Mengjun;Gu, Jingmin
由于抗生素耐药菌株在世界范围内普遍存在，噬菌体疗法最近重新焕发活力。在这项研究中，从医院污水中分离出了一种名为IME-EFm5的屎肠球菌噬菌体。全基因组序列分析表明，IME-EFm5属于Siphoviridae家族，具有42,265 bp的双链基因组（G+C含量为35.51%），包含70个推定编码序列。 LysEFm5是IME-EFm5的内溶素，其N端含有酰胺酶结构域，比其亲本噬菌体IME-EFm5具有更广泛的杀菌谱，包括7株耐万古霉素的屎肠球菌。诱变分析表明，锌离子结合残基（H27、H132 和 C140）、E90 和 T138 是 LysEFm5 催化所必需的。然而，LysEFm5 的抗菌活性不依赖于锌离子，这与大多数其他酰胺酶成员不一致。噬菌体溶素 LysEFm5 可能是治疗由多重耐药屎肠球菌引起的感染的替代治疗策略。 (C) 2016 Elsevier Inc. 保留所有权利。
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 42,265 bp (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. (C) 2016 Elsevier Inc. All rights reserved.