Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci.

Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci.
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DOI:
10.1111/1751-7915.12166
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发表时间:
2015-03
影响因子:
5.7
通讯作者:
Wei H
Wei H
中科院分区:
工程技术2区
文献类型:
--
作者:
Dong Q;Wang J;Yang H;Wei C;Yu J;Zhang Y;Huang Y;Zhang XE;Wei H

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开发具有广泛裂解谱的嵌合赖氨酸对于治疗由多种病原菌引起的一些感染将是重要的。在本工作中,通过将噬菌体溶素Ply187的催化结构域(Ply187N)和溶酶PlyV12的细胞结合区(146-314aa,V12C)融合,构建了一种新型的嵌合溶素(Ply187N-V12C)。结果表明,嵌合裂解酶Ply187N-V12C不仅对葡萄球菌具有与Ply187N相似的裂解活性,而且对Ply187N不裂解的链球菌和肠球菌如 失乳链球菌、无乳链球菌、化脓性链球菌、粪肠球菌也具有裂解活性。我们的工作表明,通过融合来自多个属的裂解谱的催化结构域和细胞结合域来产生具有扩展裂解谱的新型嵌合赖氨酸是可行的。
Developing chimeric lysins with a wide lytic spectrum would be important for treating some infections caused by multiple pathogenic bacteria. In the present work, a novel chimeric lysin (Ply187N-V12C) was constructed by fusing the catalytic domain (Ply187N) of the bacteriophage lysin Ply187 with the cell binding domain (146-314aa, V12C) of the lysin PlyV12. The results showed that the chimeric lysin Ply187N-V12C had not only lytic activity similar to Ply187N against staphylococcal strains but also extended its lytic activity to streptococci and enterococci, such as Streptococcus dysgalactiae, Streptococcus agalactiae, Streptococcus pyogenes, Enterococcus faecium and Enterococcus faecalis, which Ply187N could not lyse. Our work demonstrated that generating novel chimeric lysins with an extended lytic spectrum was feasible through fusing a catalytic domain with a cell-binding domain from lysins with lytic spectra across multiple genera.
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