STRUCTURAL CHARACTERIZATION OF THE INTERACTION BETWEEN STREPTOCOCCAL M1 PROTEIN

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 链球菌中毒性休克综合征（STSS）是由A组链球菌（GAS）引起的一种危及生命的疾病，其毒力主要是由于表面卷曲螺旋M1蛋白的存在。GAS侵入宿主细胞并引起STSS的能力取决于M1结合人纤维蛋白原并随后诱导血管渗漏的能力。这两种成分的单个结构是已知的，但为了在分子水平上了解STSS的机制，我们建议使用X射线晶体学研究M1片段和人纤维蛋白原之间的复合物。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Streptococcal Toxic Shock Syndrome (STSS) is a life-threatening disease caused by Group A Streptococcus (GAS) for which the virulence is mainly due to the presence of the surface coiled-coil M1 protein. The ability of GAS to invade host cells and cause STSS is dependent on the ability of M1 to bind human fibrinogen and subsequently induce vascular leakage. The individual structures of both components are already known but in order to understand the mechanisms of STSS at a molecular level, we propose to study the complex between M1 fragments and human fibrinogen using x-ray crystallography.