STRUCTURAL CHARACTERIZATION OF THE INTERACTION BETWEEN STREPTOCOCCAL M1 PROTEIN

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 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的M1蛋白的存在。GAS侵袭宿主细胞并引起STSS的能力取决于M1与人纤维蛋白原结合并随后导致血管渗漏的能力。这两个组分的单独结构已经知道，但为了在分子水平上了解STSS的机制，我们建议用X射线结晶学研究M1片段与人纤维蛋白原之间的复合体。

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.