Inhibition of the Activity of Both Domains of Lysostaphin through Peptidoglycan Modification by the Lysostaphin Immunity Protein
Inhibition of the Activity of Both Domains of Lysostaphin through Peptidoglycan Modification by the Lysostaphin Immunity Protein
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DOI：
10.1128/aem.01066-10
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发表时间：
2010-10-01
影响因子：
4.4
通讯作者：
Sloan, Gary L.
中科院分区：
文献类型：
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作者：
Gargis, Shaw R.;Heath, Harry E.;Sloan, Gary L.
对溶葡萄球菌酶（一种葡萄球菌溶解性甘氨酰甘氨酸内肽酶）的抗性是由于FemABX样免疫蛋白在肽聚糖跨桥中插入丝氨酸代替一些甘氨酸。这些修饰抑制重组细胞壁靶向结构域的结合和溶葡萄球菌酶的重组催化结构域的催化。
Resistance to lysostaphin, a staphylolytic glycylglycine endopeptidase, is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges. These modifications inhibit both binding of the recombinant cell wall targeting domain and catalysis by the recombinant catalytic domain of lysostaphin.