期刊
FEMS MICROBIOLOGY LETTERS
卷 265, 期 1, 页码 133-139出版社
BLACKWELL PUBLISHING
DOI: 10.1111/j.1574-6968.2006.00483.x
关键词
Staphylococcus aureus; coagulase-negative staphylococcus; phi11 endolysin; peptidoglycan hydrolase; antimicrobial
类别
The Staphylococcus aureus bacteriophage phi11 endolysin has two peptidoglycan hydrolase domains (endopeptidase and amidase) and an SH3b cell wall-binding domain. In turbidity reduction assays, the purified protein can lyse untreated staphylococcal mastitis pathogens, Staphylococcus aureus and coagulase-negative staphylococci (Staphylococcus chronogenes, Staphylococcus epidermidis, Staphylococcus hyicus, Staphylococcus simulans, Staphylococcus warneri and Staphylococcus xylosus), making it a strong candidate protein antimicrobial. This lytic activity is maintained at the pH (6.7), and the 'free' calcium concentration (3 mM) of milk. Truncated endolysin-derived proteins containing only the endopeptidase domain also lyse staphylococci in the absence of the SH3b-binding domain.
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