HDL WITH SOF

HDL 与 SOF

• 批准号: 7953809
• 负责人: Henry J. Pownall
• 金额: $ 1.74万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-12-01 至 2009-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7953809
• 关键词: Apolipoprotein A-I; Binding; Complex; Computer Retrieval of Information on Scientific Projects Database; Docking; Electron Microscopy; Funding; Grant; High Density Lipoproteins; Institution; Left; Lipids; Proteins; Recruitment Activity; Research; Research Personnel; Resources; Serum; Site; Source; Surface; United States National Institutes of Health; Virulence; macromolecule; opacity factor; particle

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 serum opacity factor (SOF), a virulence determinant that clouds serum, causes HDL instability. SOF appears to catalyzes transfer of the CE of ~100,000 HDL particles (D ~ 90 ¿) into a large CE-rich microemulsion (CERM; r >1,000 ¿) leaving a new HDL-like particle, neo HDL (D ~ 20¿), and releasing lipid-free(LF) apo A-I. rSOF is a heterodivalent fusogenic protein that uses a docking site to displace apo A-I and bind to exposed CE surfaces on HDL; the resulting rSOF-HDL complex recruits additional HDL with its binding delipidation site and, through multiple fusion steps, forms a CERM. By cryo-EM we hope to confirm this interpretation of SOF activity, and uncover more information about neo-HDL and CERMs.

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， 因此可以在其他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。 链球菌血清混浊因子（SOF）是一种使血清混浊的毒力决定因子，可导致HDL不稳定。 SOF似乎催化~ 100，000 HDL颗粒（D ~ 90 <$）的CE转移到大的富含CE的微乳液中 (CERM; r > 1，000），留下新的HDL样颗粒neo HDL（D ~ 20），并释放无脂质（LF）apo A-I。rSOF是一种异二价融合蛋白，它使用对接位点取代apo A-I并与HDL上暴露的CE表面结合;产生的rSOF-HDL复合物通过其结合去脂位点招募额外的HDL，并通过多个融合步骤，形成CERM。通过冷冻电镜，我们希望证实SOF活性的这种解释，并揭示更多关于neo-HDL和CERM的信息。