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来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 研究中心，而研究中心不一定是研究者所在的机构。 我们开始了一个新的项目，与BTI康奈尔大学的加里布利萨德小组合作，研究GP 64的跨膜（TM）结构域在病毒膜融合中的作用。GP 64是苜蓿银纹夜蛾核型多角体病毒（AcMNPV）的主要糖蛋白。 Blissard等发现，GP 64的TM结构域被6种病毒包膜蛋白和2种细胞膜蛋白的相应TM结构域所取代的突变体都能诱导半融合，但只有部分突变体能完成融合活性。 为了研究膜结构的变化对这些蛋白质介导的融合活性的差异的贡献，将使用自旋标记方法来研究来自表达GP 64及其突变体的sf 9细胞的质膜囊泡（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.