首页> 外文期刊>Molecular Microbiology >Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus.
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Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus.

机译:为什么病原性葡萄球菌如此耐溶菌酶?肽聚糖O-乙酰基转移酶OatA是金黄色葡萄球菌耐溶菌酶的主要决定因素。

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摘要

Staphylococcus species belong to one of the few bacterial genera that are completely lysozyme resistant, which greatly contributes to their persistence and success in colonizing the skin and mucosal areas of humans and animals. In an attempt to discover the cause of lysozyme resistance, we identified a gene, oatA, in Staphylococcus aureus. The corresponding oatA deletion mutant had an increased sensitivity to lysozyme. HPLC and electrospray ionization tandem mass spectrometry analyses of the cell wall revealed that the muramic acid of peptidoglycan of the wild-type strain was O-acetylated at C6-OH, whereas the muramic acid of the oatA mutant lacked this modification. The complemented oatA mutant was lysozyme resistant. We identified the first bacterial peptidoglycan-specific O-acetyltransferase in S. aureus and showed that OatA, an integral membrane protein, is the molecular basis for the high lysozyme resistance in staphylococci.
机译:金黄色葡萄球菌属属于完全对溶菌酶具有抗性的少数细菌属之一,这极大地有助于其在人类和动物的皮肤和粘膜区域定居的持久性和成功。为了发现溶菌酶抗性的原因,我们在金黄色葡萄球菌中鉴定了一个基因oatA。相应的燕麦缺失突变体对溶菌酶的敏感性增加。对细胞壁的HPLC和电喷雾串联质谱分析表明,野生型菌株的肽聚糖的山mic酸在C6-OH处是O-乙酰化的,而oatA突变体的山mic酸缺乏这种修饰。互补的燕麦突变体是耐溶菌酶的。我们在金黄色葡萄球菌中鉴定了第一个细菌肽聚糖特异性的O-乙酰基转移酶,并显示OatA是必不可少的膜蛋白,是葡萄球菌中高溶菌酶抗性的分子基础。

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