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Herpes simplex virus type 1 glycoprotein B (HSV-1 gB) is a highly conserved class III viral fusion protein that is essential for the virus to enter host cells. It functions as the core component of the viral fusion machinery, working alongside glycoproteins gD, gH, and gL to mediate the merging of the viral envelope with the host cell plasma or endosomal membranes. Beyond its role in initial entry, gB is critical for cell-to-cell spread and the formation of multinucleated syncytia, which are hallmarks of herpesvirus pathogenesis. Because it is a prominent surface protein, gB is a primary target for neutralizing antibodies and a major focus for vaccine development and entry-inhibitor therapeutics. Drugs like docosanol are thought to interfere with the fusion process facilitated by gB, while experimental monoclonal antibodies and peptides aim to stabilize the protein in its pre-fusion conformation to prevent infection.
Fusion inhibition, neutralization of viral particles, and blocking of viral attachment to host cell receptors.
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