ERICA OLLMANN SAPHIRE PRT TIME

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.