ULTRASTRUCTURAL LOCALIZATION OF THE HOST ANTIVIRAL PROTEIN BST-2

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。 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. 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.