TRANSMEMBRANE DOMAIN FROM INFLUENZA HEMAGGLUTININ/MEMBRANE INTERACTIONS

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。 我们开始研究一种与流感病毒血凝素(HA)的跨膜区(TM)相对应的合成肽的脂质相互作用。我们对TM是扮演被动角色还是主动参与HA介导膜融合的问题很感兴趣。最近有研究表明，用糖基磷脂醇连接的脂质锚取代HA的TM可以导致半融合，但不是完全融合。同时，用单一的脂质单位取代v-SNARE或T-SNARE(或两者)的多肽锚定，可阻止SNARE介导的囊泡融合中的脂质混合。结果表明，仅仅将两个囊泡保持在一起是不足以实现膜融合的，对膜锚定施加的拉力可能是膜融合活性的重要因素。

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 initiated a study of lipid interactions of a synthetic peptide corresponding to the transmembrane domain (TM) of hemagglutinin (HA) from influenza virus. We are intrigued by a question of whether the TM plays a passive role, or is actively involved in HA-mediated membrane fusion. Recently it was shown that replacing the TM of HA with a glycophosphoinositol-linked lipid anchor results in hemifusion, but not complete fusion. Also replacing either the v-SNARE or t-SNARE (or both) peptidic anchors with a single lipid unit, prohibits lipid mixing in SNARE-mediated vesicle fusion. It was suggested that simply holding two vesicles together is not sufficient for membrane fusion, and a pulling force exerted on the membrane anchors might be important for the fusion activity.