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Enveloped viruses enter cells via receptor-dependent mechanisms that involve specific events in the cell membrane. The entry mechanisms of influenza virus and herpes simplex virus (HSV), for example, are distinct. Influenza virus attaches to sialic acid receptors via hemagglutinin (HA) and fuses to membranes via fusion (F) protein. Cells can resist infection by interfering with the viral fusion process. Herpes simplex virus (HSV) is thought to be analogous to influenza virus with respect to its entry mechanism. However, although many details of HSV entry are known, the fusion process is still not well understood. During fusion, viral glycoproteins insert into the cell membrane by a unique pathway in which the negative membrane charges of the membrane are partially neutralized by insertion into the membrane. This pathway is independent of plasma membrane fluidity and appears to be specific for the fusion process. Furthermore, the mechanism of this insertion appears to involve “ballooning” in two-dimensional sheets, which forms the basis of the “two step” model of the membrane fusion process. This process involves the formation of an early, hemifusion intermediate. This process, in turn, is thought to promote a late, fusion event in which the two lipid bilayers join. In vivo, such fusion intermediates might have a protective function. This proposal has two main objectives. First, the “ballooning” process will be characterized further. Specific questions to be addressed include the identity of viral glycoproteins that promote membrane “ballooning,” the clustering of glycoproteins required for the formation of the membrane balloons, and the source of the calcium that is needed to initiate the membrane-ballooning process. A related aim of the proposal is to determine the energetics of the membrane “ballooning” process. Most proteins that can bind and unfold membrane will unfold a “flat” membrane. For proteins with high affinity for membrane, the energy cost of unfolding must be smaller than the energetic cost of unfolding a membrane that is free of protein. This will be accomplished by developing assays for probing the spatial arrangement of proteins in the plane

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