Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin.

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 Lett

authors

Donovan DM,Lardeo M,Foster-Frey J

doi

10.1111/j.1574-6968.2006.00483.x

subject

Has Abstract

pub_date

2006-12-01 00:00:00

pages

133-9

issue

1

eissn

0378-1097

issn

1574-6968

pii

FML483

journal_volume

265

pub_type

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