ULTRASTRUCTURAL LOCALIZATION OF THE HOST ANTIVIRAL PROTEIN BST-2

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 而子项目的主要调查员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。 干扰素诱导的宿主蛋白BST-2（也称为HM 1.24，CD 317和tetherin）最近被发现作为一种抗病毒因子，限制新形成的病毒颗粒从感染细胞中释放。HIV-1编码一种特异性蛋白Vpu，它可以对抗这种限制。 BST-2与特定细胞膜系统和形成病毒颗粒相关的超微结构分布尚不清楚。 我们打算用相关的光镜和电镜免疫定位技术来确定这一点。 这些实验有望揭示BST-2限制病毒复制的机制以及HIV-1抵消这种限制的机制。

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 interferon-induced host protein BST-2 (also known as HM1.24, CD317, and tetherin) has recently been found to function as an antiviral factor that restricts the release of newly formed virus particles from infected cells. HIV-1 encodes a specific protein, Vpu, that antagonizes this restriction. The ultrastructural distribution of BST-2 in relation to specific cellular membrane systems and forming virus particles is unknown. We intend to determine this using correlative light and electron microscopic immuno-localization techniques. These experiments are expected to reveal aspects of the mechanism by which BST-2 restricts viral replication and the mechanism by which HIV-1 counteracts this restriction.