Abstract:
: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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Donovan DM,Lardeo M,Foster-Frey Jdoi
10.1111/j.1574-6968.2006.00483.xsubject
Has Abstractpub_date
2006-12-01 00:00:00pages
133-9issue
1eissn
0378-1097issn
1574-6968pii
FML483journal_volume
265pub_type
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