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

• Published in: Microbial biotechnology 2015-03, Vol.8 (2), p.210-220
• Main Authors: Dong, Qiuhua, Wang, Jing, Yang, Hang, Wei, Cuihua, Yu, Junping, Zhang, Yun, Huang, Yanling, Zhang, Xian‐En, Wei, Hongping
• Format: Article
• Language: English
• Subjects: Bacteriolysis; Catalytic Domain - genetics; Enterococcus - drug effects; Enterococcus faecalis; Enterococcus faecium; Mucoproteins - genetics; Mucoproteins - metabolism; Protein Binding; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Staphylococcus - drug effects; Streptococcus - drug effects; Streptococcus agalactiae; Streptococcus pyogenes; Substrate Specificity; Viral Proteins - genetics; Viral Proteins - metabolism
• ISSN: 1751-7915; 1751-7915
• DOI: 10.1111/1751-7915.12166

Summary 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. 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. Our work demonstrated that the generating novel chimeric lysin with an extended lytic spectrum was feasible through fusing catalytic domain with cell binding domains from lysins with lytic spectra across multiple genera.