ERICA OLLMANN SAPHIRE PRT TIME

埃丽卡·奥尔曼 SAPHIRE PRT 时间

• 批准号: 8362062
• 负责人: Erica Ollmann Saphire
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362062
• 关键词: Amino Acids; Antibodies; C-terminal; Cells; Ebola virus; Event; Funding; Genes; Glycoproteins; Grant; N-terminal; National Center for Research Resources; Pathogenesis; Pathogenicity; Pattern; Principal Investigator; Proteins; Radiation; Research; Research Infrastructure; Resources; Role; Source; Structure; Surface; Time; Tropism; United States National Institutes of Health; Vaccine Design; Viral; Virus; comparative; cost; dimer; disulfide bond; structural biology

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.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 子项目的主要研究者可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子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。