The Staphylococcus aureus extracellular matrix protein (Emp) has a fibrous structure and binds to different extracellular matrices.

The Staphylococcus aureus extracellular matrix protein (Emp) has a fibrous structure and binds to different extracellular matrices.
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DOI:
10.1038/s41598-017-14168-4
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发表时间:
2017-10-20
期刊:
影响因子:
4.6
通讯作者:
Tuchscherr L
Tuchscherr L
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Geraci J;Neubauer S;Pöllath C;Hansen U;Rizzo F;Krafft C;Westermann M;Hussain M;Peters G;Pletz MW;Löffler B;Makarewicz O;Tuchscherr L

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金黄色葡萄球菌的细胞外基质蛋白Emp是一种分泌的粘附素,介导细菌表面和细胞外宿主结构之间的相互作用。然而,它的结构和葡萄球菌发病机制中的作用仍然未知。使用多学科的方法,包括圆二色性(CD)和傅里叶变换红外(FTIR)光谱,透射电子显微镜(TEM)和免疫金透射电子显微镜,功能ELISA测定和计算机技术,我们的特点是Emp蛋白。我们证明,EMP及其截短形式结合到人体皮肤,软骨或骨中的超结构,其中皮肤化合物的结合活性似乎更高。结合结构域位于蛋白质的C末端部分。CD光谱显示高含量的β-折叠(39.58%)和天然无序结构(41.2%),TEM显示由Emp聚合物组成的纤维状结构。N-末端似乎是聚合所必需的。由于不寻常的高组氨酸含量,我们建议,EMP代表一种新型的富含组氨酸的蛋白质共享结构相似的富含亮氨酸的重复序列的蛋白质预测的I-TASSER算法。这些新发现表明EMP在更深组织感染中的作用,并为开发新的治疗策略开辟了新的可能性。
The extracellular matrix protein Emp of Staphylococcus aureus is a secreted adhesin that mediates interactions between the bacterial surface and extracellular host structures. However, its structure and role in staphylococcal pathogenesis remain unknown. Using multidisciplinary approaches, including circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy, transmission electron (TEM) and immunogold transmission electron microscopy, functional ELISA assays and in silico techniques, we characterized the Emp protein. We demonstrated that Emp and its truncated forms bind to suprastructures in human skin, cartilage or bone, among which binding activity seems to be higher for skin compounds. The binding domain is located in the C-terminal part of the protein. CD spectroscopy revealed high contents of β-sheets (39.58%) and natively disordered structures (41.2%), and TEM suggested a fibrous structure consisting of Emp polymers. The N-terminus seems to be essential for polymerization. Due to the uncommonly high histidine content, we suggest that Emp represents a novel type of histidine-rich protein sharing structural similarities to leucine-rich repeats proteins as predicted by the I-TASSER algorithm. These new findings suggest a role of Emp in infections of deeper tissue and open new possibilities for the development of novel therapeutic strategies.
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