POLYOMA VIRUS REPLICATION

多瘤病毒复制

• 批准号: 8362556
• 负责人: Robert L Garcea
• 金额: $ 3.19万
• 依托单位: UNIVERSITY OF COLORADO
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-05-01 至 2012-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362556
• 关键词: 3T3 Cells; Apoptosis; Caliber; Capsid; Capsid Proteins; Cell Cycle Progression; Cell Nucleus; Cell physiology; Cells; Cellular Structures; Collaborations; DNA biosynthesis; Data; Funding; Gene Expression; Goals; Grant; Large T Antigen; Mus; National Center for Research Resources; Nuclear; Phase; Polyomavirus; Principal Investigator; Process; Proteins; Research; Research Infrastructure; Resources; S Phase; Source; Structural Protein; United States National Institutes of Health; Viral; Viral Nonstructural Proteins; Virion; Virus; Virus Replication; cost; immunocytochemistry; migration; particle; prevent; viral DNA

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. Murine PyV is a double stranded, none enveloped virus. Its capsid (50 nm in diameter) is composed of 72 pentamers of the major coat protein VP1 and of VP2 and VP3 proteins buried within the capsid. After entry and migration to the cell host nucleus, the mPyV gene expression can be divided into two phases (3, 4). The early phase sees nonstructural viral proteins such as small, middle and large T antigen to be synthesized. Those proteins highly interact with the host cell key proteins. As a result, the virus takes control of cellular mechanisms like; cell cycle progression towards S-phase as well as preventing the cell to engage apoptosis process. The early phase leads to viral DNA replication exploiting the host nuclear machinery. During the later phase, the structural proteins (VP1, VP2, VP3) are expressed and de novo viral particles are assembled in the nucleus. The goal of the collaboration is to combine immunocytochemistry data on EM prepared infected 3T3 cells coming from the Garcea lab and ultrastructural information collected in the facility to understand better the way Polyoma virus particles assembled in the cell nucleus as well as how PML bodies are involved in this process.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 鼠 PyV 是一种双链、无包膜病毒。其衣壳（直径 50 nm）由主要外壳蛋白 VP1 以及埋藏在衣壳内的 VP2 和 VP3 蛋白的 72 个五聚体组成。进入并迁移至细胞宿主细胞核后，mPyV 基因表达可分为两个阶段（3、4）。早期阶段会合成非结构病毒蛋白，例如小、中和大 T 抗原。这些蛋白质与宿主细胞关键蛋白质高度相互作用。结果，病毒控制了细胞机制，例如：细胞周期进展至S期并阻止细胞参与凋亡过程。早期阶段导致病毒 DNA 利用宿主核机制进行复制。在后期，结构蛋白（VP1、VP2、VP3）被表达，并且从头病毒颗粒在细胞核中组装。此次合作的目标是将来自 Garcea 实验室的 EM 制备的感染 3T3 细胞的免疫细胞化学数据与该设施中收集的超微结构信息结合起来，以更好地了解多瘤病毒颗粒在细胞核中组装的方式以及 PML 体如何参与这一过程。