CHARACTERIZATION OF INFLUENZA VIRUS HEMAGGLUTININ (HA) IN COMPLEX WITH LIPOSOMES

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。 被包裹的病毒使用特殊的蛋白质机制，以编程的方式将病毒膜与宿主细胞的膜融合。甲型流感病毒是一种通过受体介导的内吞作用了解病毒进入宿主细胞的范例。血凝素(HA)包膜糖蛋白介导流感病毒膜融合。虽然HA介导的融合的某些方面已经被表征，但在实际驱动膜融合的分子构象的结构表征、我们对HA如何切换构象以及HA构象变化和膜变形之间的相互作用的理解方面仍然存在显著的差距。

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. Enveloped viruses use specialized protein machinery to fuse the viral membrane with that of the host cell in a programmed fashion. Influenza A virus is a paradigm for understanding viral entry of host cells via receptor-mediated endocytosis. The hemagglutinin (HA) envelope glycoprotein mediates influenza virus membrane fusion. While certain facets of HA-mediated fusion have been characterized, significant gaps remain in the structural characterization of the molecular conformations that actually drive membrane fusion, in our understanding of how HA switches conformations, and in our understanding of the interplay between HA conformational change and membrane deformation.