Open AccessConstruction of a chimeric lysin Ply187N ‐ V12C with extended lytic activity against staphylococci and streptococci
Author(s) -
Dong Qiuhua,
Wang Jing,
Yang Hang,
Wei Cuihua,
Yu Junping,
Zhang Yun,
Huang Yanling,
Zhang XianEn,
Wei Hongping
Publication year - 2015
Publication title -
microbial biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.287
H-Index - 74
ISSN - 1751-7915
DOI - 10.1111/1751-7915.12166
Subject(s) - lysin , lytic cycle , microbiology and biotechnology , bacteriophage , streptococcus pyogenes , enterococcus faecium , biology , streptococcus agalactiae , enterococcus faecalis , streptococcus dysgalactiae , enterococcus , streptococcus , virology , bacteria , staphylococcus aureus , antibiotics , escherichia coli , genetics , virus , gene
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 P ly187 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 S treptococcus dysgalactiae , S treptococcus agalactiae , S treptococcus pyogenes , E nterococcus faecium and E nterococcus 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.