Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin
2006; Oxford University Press; Volume: 265; Issue: 1 Linguagem: Inglês
10.1111/j.1574-6968.2006.00483.x
ISSN1574-6968
AutoresDavid M. Donovan, Michelle Lardeo, Juli Foster‐Frey,
Tópico(s)Milk Quality and Mastitis in Dairy Cows
ResumoThe 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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