TRANSMEMBRANE DOMAIN FROM INFLUENZA HEMAGGLUTININ/MEMBRANE INTERACTIONS

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。子项目及 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。 我们开始了流感病毒血凝素（HA）跨膜结构域（TM）的合成肽的脂质相互作用的研究。我们感兴趣的一个问题，TM是否发挥了被动作用，或积极参与HA介导的膜融合。 最近显示，用糖磷酸肌醇连接的脂质锚代替HA的TM导致半融合，但不完全融合。此外，用单个脂质单元替换v-SNARE或t-SNARE（或两者）肽锚，阻止了SNARE介导的囊泡融合中的脂质混合。有人提出，简单地将两个囊泡保持在一起不足以进行膜融合，并且施加在膜锚上的拉力对于融合活性可能是重要的。

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.