ERICA OLLMANN SAPHIRE PRT TIME

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。 埃博拉病毒糖蛋白Sgp和gp是病毒致病性的主要决定因素。Sgp和gp由同一个基因编码，N-末端序列共有295个氨基酸。然而，转录编辑事件会导致它们具有不同的C-末端序列。不同的C末端导致不同的二硫键模式、不同的结构和不同的致病作用。SGP形成一种反平行二聚体，由感染细胞大量分泌。GP在病毒表面形成一个平行的三聚体，在病毒的附着、融合和趋向性中发挥作用。SGP和GP的比较结构分析应该解释两种结构是如何从同一序列产生的，并提供模板来指导疫苗的设计，这些疫苗诱导针对病毒而不是分泌蛋白的抗体。

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. The Ebola virus glycoproteins, sGP and GP, are major determinants of the virus's pathogenicity. sGP and GP are encoded by the same gene, and thus share 295 amino acids of N-terminal sequence. However, a transcriptional editing event causes them to have different C-terminal sequences. The different C termini result in unique patterns of disulfide bonding, different structures, and different roles in pathogenesis. sGP forms an antiparallel dimer and is secreted in large quantities from infected cells. GP forms a parallel trimer on the viral surface, and functions in viral attachment, fusion, and tropism. Comparative structural analysis of sGP and GP should explain how two structures arise from the same sequence, and provide templates to guide the design of vaccines that elicit antibodies which target the virus rather than the secreted proteins.