ESR STUDIES OF DYNAMIC STRUCTURES OF PLASMA MEMBRANE VESICLES FROM SF9 CELLS

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。 我们与BTI Cornell的Gary Blissard小组合作启动了一个新项目，以研究GP64的跨膜(TM)结构域在病毒膜融合中的作用。核型多角体病毒(AcMNPV)的主要糖蛋白是GP64。Blissard和他的同事们发现，用6种病毒囊膜蛋白和2种细胞膜蛋白的TM结构域替换GP64的TM结构域的突变体都可以诱导半融合，但只有部分突变体可以完成融合活性。为了研究膜结构的改变对这些蛋白介导的融合活性差异的贡献，我们将用自旋标记方法研究表达GP64及其突变体的sf9细胞来源的质膜小泡(PMV)的动态结构。

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. We started a new project, in collaboration with the Gary Blissard group at BTI Cornell, to investigate the role of the transmembrane (TM) domain of GP64 for viral membrane fusion. GP64 is the major glycoprotein in autographa californica multicapsid nucleopolyhedrovirus (AcMNPV). Blissard and his coworkers found that mutants of GP64 in which the TM domain of GP64 was substituted with corresponding TM domains from six viral envelope proteins and two cellular membrane proteins could all induce hemifusion, but only some of the mutants could complete fusion activities. To examine what is the contribution of changes in the membrane structure to the differences in the fusion activities mediated by these proteins, the spin labeling method will be used to study the dynamic structures of plasma membrane vesicles (PMV) derived from sf9 cells in which GP64 and its mutants are expressed.