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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family
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ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family

机译:ErpC是来自伯氏疏螺旋体的补体调节剂表面​​蛋白家族的成员,其结构在该蛋白家族中尚属未知

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摘要

Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts.
机译:伯氏疏螺旋体是引起莱姆病的一种螺旋体,莱姆病是欧洲和北美最常见的媒介传播疾病。该细菌利用一组称为补体调节剂的表面蛋白(CRASPs)的蛋白质,通过以模拟宿主细胞的方式在其表面募集并呈递补体调节因子H来帮助逃避人类补体系统。这里介绍的是此蛋白质家族ErpC成员的原子拆分结构。该结构通过充当宿主糖胺聚糖的分子模拟物,为募集因子H和其他因子H相关蛋白的机制提供了新见解。它还描述了属于OspE / F相关旁系蛋白家族的其他CRASP蛋白的结构,并暗示它们已经进化为结合特异性补体蛋白,从而有助于细菌在不同宿主中的存活。

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