Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin

被引：112

作者：

Donovan, David M. ^{[1
]}

Lardeo, Michelle ^{[1
]}

Foster-Frey, Juli ^{[1
]}

机构：

[1] USDA ARS, Biotechnol & Germplasm Lab, ANRI, Beltsville, MD 20705 USA

来源：

FEMS MICROBIOLOGY LETTERS | 2006年 / 265卷 / 01期

关键词：

Staphylococcus aureus; coagulase-negative staphylococcus; phi11; endolysin; peptidoglycan hydrolase; antimicrobial;

D O I：

10.1111/j.1574-6968.2006.00483.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：133 / 139

页数：7

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