Identification and preliminary characterization of cell-wall-anchored proteins of Staphylococcus epidermidis
Identification and preliminary characterization of cell-wall-anchored proteins of Staphylococcus epidermidis
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DOI：
10.1099/mic.0.27534-0
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发表时间：
2005-05-01
期刊：
影响因子：
2.8
通讯作者：
Höök, M
中科院分区：
文献类型：
--
作者：
Bowden, MG;Chen, W;Höök, M
表皮葡萄球菌是一种普遍存在的人类皮肤真菌，已成为异物感染的主要原因。通过计算机分析公开的S.表皮未完成的基因组序列。四个基因编码先前描述的蛋白质（Aap，Bhp，SdrF和SdrG），而其余七个尚未被表征。对表皮葡萄球菌表面（Ses）蛋白一级序列的分析表明，它们具有与先前描述的来自S.金黄色葡萄球菌和其他革兰氏阳性球菌。然而，并非所有的Ses蛋白都是S.金黄色葡萄球菌蛋白。二级和三级结构的预测表明，大多数的Ses蛋白是由几个连续的子域，这些预测的子域中的大多数折叠成富含β的结构。PCR分析表明，与从健康皮肤分离的菌株相比，某些基因可能在疾病分离株中更频繁地被发现。患者从S.表皮葡萄球菌感染对某些Ses蛋白具有较高的抗体滴度，这意味着这些蛋白在人类感染期间表达。早期对数和晚期静止的体外培养的Western印迹分析表明，不同的调节机制控制的Ses蛋白的表达。
Staphylococcus epidermidis is a ubiquitous human skin commensal that has emerged as a major cause of foreign-body infections. Eleven genes encoding putative cell-wall-anchored proteins were identified by computer analysis of the publicly available S. epidermidis unfinished genomic sequence. Four genes encode previously described proteins (Aap, Bhp, SdrF and SdrG), while the remaining seven have not been characterized. Analysis of primary sequences of the Staphylococcus epidermidis surface (Ses) proteins indicates that they have a structural organization similar to the previously described cell-wail-anchored proteins from S. aureus and other Gram-positive cocci. However, not all of the Ses proteins are direct homologues of the S. aureus proteins. Secondary and tertiary structure predictions suggest that most of the Ses proteins are composed of several contiguous subdomains, and that the majority of these predicted subdomains are folded into beta-rich structures. PCR analysis indicates that certain genes may be found more frequently in disease isolates compared to strains isolated from healthy skin. Patients recovering from S. epidermidis infections had higher antibody titres against some Ses proteins, implying that these proteins are expressed during human infection. Western blot analyses of early-logarithmic and late-stationary in vitro cultures suggest that different regulatory mechanisms control the expression of the Ses proteins.