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Herpes simplex virus (HSV) entry into host cells is critically dependent on the fusion of the viral envelope with the host cell membrane. This process allows delivery of the viral nucleocapsid and tegument proteins into the cytoplasm, initiating infection. The fusion event is mediated by a set of specialized viral glycoproteins embedded in the HSV envelope, which interact with specific receptors on the host cell surface. Key glycoproteins involved are gB (the main fusogen), gD (receptor binding and trigger), and the gH/gL complex (required for full fusion activity). The process involves attachment, triggering conformational changes, and fusion execution, ultimately leading to the release of the nucleocapsid into the cytosol. Cholesterol within both viral envelope and target cell plasma membrane facilitates efficient membrane merging. Blocking this step prevents HSV entry into cells, making it a prime target for antiviral drug development.
Inhibition of viral entry by preventing membrane fusion.
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