Peer-reviewed veterinary case report
Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin.
- Journal:
- FEMS microbiology letters
- Year:
- 2006
- Authors:
- Donovan, David M et al.
- Affiliation:
- US Department of Agriculture · United States
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.
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Search related cases →Original publication: https://pubmed.ncbi.nlm.nih.gov/17054440/