HEPATITUS C P7 VIROPORIN

丙型肝炎 P7 病毒孔蛋白

• 批准号: 8363667
• 负责人: DARRELL P CHANDLER
• 金额: $ 3.32万
• 依托单位: UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-08-01 至 2012-09-09
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363667
• 关键词: Amino Acids; Bioinformatics; Cations; Charge; Chronic Hepatitis; Complex; Data; Endoplasmic Reticulum; Environment; Flowers; Funding; Grant; Hepatitis C; Hepatitis C virus; Hepatitis C virus p7 protein; Integral Membrane Protein; Ion Channel; Lipids; Liver Cirrhosis; Maps; Modeling; National Center for Research Resources; Primary carcinoma of the liver cells; Principal Investigator; Reporting; Research; Research Infrastructure; Resolution; Resources; Source; Structure; Tail; United States National Institutes of Health; Virion; base; cost; global health; monomer

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. Hepatitis C virus (HCV) infection is a major, global health problem and a leading cause of chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. The HCV p7 protein is a small integral membrane protein of 63 amino acids which oligomerizes and forms cation-selective pores. It has recently been demonstrated that p7 ion channel activity is required for the effective assembly and release of nascent HCV virions [1]. There is no crystal structure of p7, however, models based on experimental data have been explored. The p7 monomer forms two antiparallel transmembrane segments connected by a conserved cytosolic charged loop region, with both the N- and C-termini facing the lumen of the endoplasmic reticulum [2]. p7 oligomers have been observed in both heptameric and hexameric forms [3, 4, 5], and several hypothetical models of the p7 complex based on secondary-structure predictions have been reported [6, 3, 5, 7]. Most recently, a low-resolution cryo- EM map of p7 in a short-tail lipid environment (DHPC) by Luik et al. revealed a flower-like hexameric structure [5].

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 丙型肝炎病毒（HCV）感染是一个主要的全球健康问题，是领先的 慢性肝炎，肝硬化和肝细胞癌的原因。 HCV P7蛋白是63个氨基酸的小型整合膜蛋白 并形成阳离子选择性孔。最近已经证明了P7 离子通道活性是有效组装和新生释放所必需的 HCV病毒体[1]。但是，没有P7的晶体结构，基于模型 已经探索了实验数据。 P7单体形成两个反平行 由保守的胞质电荷区域连接的跨膜段， N-和C-termini都面对内质网的腔内[2]。 在七聚体和六聚体形式中都观察到P7低聚物[3,4,5]， 以及基于二级结构的P7复合物的几种假设模型 已经报道了预测[6，3，5，7]。最近，低分辨率的冷冻 Luik等人的短尾脂质环境（DHPC）中P7的EM图。揭示了 花样六聚体结构[5]。