ERICA OLLMANN SAPHIRE PRT TIME

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。 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由相同的基因编码，因此共享N-末端序列的295个氨基酸。然而，转录编辑事件导致它们具有不同的C-末端序列。不同的C末端导致独特的二硫键模式、不同的结构和在发病机制中的不同作用。sGP形成反平行二聚体，并从感染细胞中大量分泌。 GP在病毒表面形成平行的三聚体，并在病毒附着、融合和向性中起作用。 sGP和GP的比较结构分析应该解释两种结构是如何从相同的序列中产生的，并提供模板来指导疫苗的设计，这些疫苗可以引发靶向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.