Journal
MICROBIAL BIOTECHNOLOGY
Volume 8, Issue 2, Pages 210-220Publisher
WILEY-BLACKWELL
DOI: 10.1111/1751-7915.12166
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Funding
- Basic Research Program of the Ministry of Science and Technology of China [2012CB721102]
- Key Laboratory on Emerging Infectious Diseases and Biosafety in Wuhan
- Institute of Biophysics
- National Laboratory of Biomacromolecules
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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 Streptococcusdysgalactiae, 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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