Construction of a chimeric lysin Ply187N‐V12C with extended lytic activity against staphylococci and streptococci. Issue 2 (15th September 2014)

• Record Type: Journal Article
• Authors: Dong, Qiuhua; Wang, Jing; Yang, Hang; Wei, Cuihua; Yu, Junping; Zhang, Yun; Huang, Yanling; Zhang, Xian‐En; Wei, Hongping
• Is Part Of: Microbial biotechnology. Volume 8:Issue 2(2015:Mar.)
• Page Start: 210
• Page End: 220
• Publication Date: 2014-09-15
• Subjects: Microbial biotechnology -- Periodicals; Biotechnology; Microbiology; 660.62
• DOI: 10.1111/1751-7915.12166
• Languages: English
• ISSNs: 1751-7915

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>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 <italic>S</italic><italic>treptococcus dysgalactiae</italic>, <italic>S</italic><italic>treptococcus agalactiae</italic>, <italic>S</italic><italic>treptococcus pyogenes</italic>, <italic>E</italic><italic>nterococcus faecium</italic> and <italic>E</italic><italic>nterococcus faecalis</italic>, 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.</p> </abstract>