ULTRASTRUCTURAL LOCALIZATION OF THE HOST ANTIVIRAL PROTEIN BST-2

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 干扰素诱导的宿主蛋白BST-2(也称为HM1.24、CD317和Tetherin)最近被发现具有抗病毒因子的功能，限制新形成的病毒颗粒从感染细胞中释放。HIV-1编码一种特殊的蛋白质VPU，它可以对抗这种限制。BST-2在特定细胞膜系统和形成病毒颗粒中的超微结构分布尚不清楚。我们打算使用相关的光和电子显微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. 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. 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.