title: Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci.
abstract: 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.
authors.affiliation: Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, 430074, China; Center for Emerging Infectious Diseases, Key Laboratory of Special Pathogens and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China.
authors.forename: Qiuhua
authors.initials: Q
authors.lastname: Dong
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.forename: Hang
authors.initials: H
authors.lastname: Yang
authors.forename: Cuihua
authors.initials: C
authors.lastname: Wei
authors.forename: Junping
authors.initials: J
authors.lastname: Yu
authors.forename: Yun
authors.initials: Y
authors.lastname: Zhang
authors.forename: Yanling
authors.initials: Y
authors.lastname: Huang
authors.forename: Xian-En
authors.initials: XE
authors.lastname: Zhang
authors.forename: Hongping
authors.initials: H
authors.lastname: Wei
mesh_terms: D001433:Bacteriolysis; D020134:Catalytic Domain / Q000235:genetics; D016983:Enterococcus / Q000187:drug effects*; D009088:Mucoproteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D013210:Staphylococcus / Q000187:drug effects*; D013291:Streptococcus / Q000187:drug effects*; D013379:Substrate Specificity; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D009088:Mucoproteins; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; C010393:lysin, gastropoda