Open AccessChimeric P ly187 endolysin kills S taphylococcus aureus more effectively than the parental enzyme
Author(s) -
Mao Jinzhe,
Schmelcher Mathias,
Harty William J.,
FosterFrey Juli,
Donovan David M.
Publication year - 2013
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12104
Subject(s) - lysin , staphylococcus aureus , peptidoglycan , microbiology and biotechnology , endopeptidase , enzyme , fusion protein , staphylococcus , biology , chemistry , biochemistry , bacteria , bacteriophage , escherichia coli , recombinant dna , gene , genetics
Peptidoglycan hydrolases are an effective new source of antimicrobials. A chimeric fusion protein of the P ly187 endopeptidase domain and L ys K SH 3b cell wall–binding domain is a potent agent against S taphylococcus aureus in four functional assays.