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Herpesvirus surface glycoproteins are a diverse group of proteins embedded in the lipid envelope of viruses in the Herpesviridae family, including Herpes Simplex Virus (HSV), Varicella-Zoster Virus (VZV), and Cytomegalovirus (CMV) (PubMed: 22440971). These proteins, such as glycoprotein B (gB), gD, gH, and gL, are essential for the viral life cycle, mediating attachment to host cell receptors and facilitating the fusion of the viral envelope with the host cell membrane (PubMed: 24503071). Beyond entry, some glycoproteins play roles in cell-to-cell spread and immune evasion by interfering with host complement or antibody functions (PubMed: 22440971). Because they are exposed on the virion surface and are critical for infectivity, they are primary targets for neutralizing antibodies, recombinant vaccines like Shingrix which targets VZV gE, and entry-inhibitor drugs like Docosanol (FDA, 2017; PubChem CID 12620). Targeting these glycoproteins aims to prevent initial infection, reduce viral shedding, and limit the reactivation of latent viruses. However, challenges include the high diversity of these proteins across the herpesvirus family and the inability to target the latent viral reservoir (PubMed: 31645451).
Neutralization of viral particles, inhibition of viral attachment to host receptors, and blockade of membrane fusion between the viral envelope and the host cell membrane.
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