Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin
Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin
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DOI：
10.1111/j.1574-6968.2006.00483.x
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发表时间：
2006-12-01
影响因子：
2.1
通讯作者：
Foster-Frey, Juli
中科院分区：
文献类型：
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作者：
Donovan, David M.;Lardeo, Michelle;Foster-Frey, Juli
金黄色葡萄球菌噬菌体phi11内溶素具有两个肽聚糖水解酶结构域（内肽酶和氨基酶）和一个SH3b细胞壁结合结构域。在降浊试验中，纯化后的蛋白可以裂解未经处理的乳腺炎葡萄球菌病原体、金黄色葡萄球菌和凝固酶阴性葡萄球菌（慢生葡萄球菌、表皮葡萄球菌、葡萄球菌、拟合葡萄球菌、warneri葡萄球菌和木糖葡萄球菌），是一种很强的候选抗菌蛋白。在牛奶的pH值（6.7）和“游离”钙浓度（3mm）下，这种分解活性保持不变。截断的仅含有内肽酶结构域的内溶素衍生蛋白在缺乏sh3b结合结构域的情况下也能裂解葡萄球菌。
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.