Viral surface glycoprotein

Viral surface glycoproteins are critical structural components of enveloped viruses that reside on the exterior of the virion, where they mediate the initial stages of the viral life cycle. These proteins are primarily responsible for recognizing and binding to specific receptors on the host cell surface, followed by the orchestration of membrane fusion to allow the viral genome to enter the cytoplasm (PMID: 31513344). Because they are the most exposed viral elements, they serve as the principal targets for the host's neutralizing antibody response and are the primary antigens used in vaccine development (PMID: 35711413). To survive immune pressure, many viral glycoproteins have evolved mechanisms such as high mutation rates (antigenic drift) and extensive N-linked glycosylation, known as glycan shielding, which masks conserved epitopes from antibody recognition (PMID: 17307400). Therapeutic strategies targeting these proteins include monoclonal antibodies that neutralize the virus, small molecule inhibitors that block attachment or fusion, and lectins that bind to surface glycans (PMID: 12633313). Prominent examples include the Spike protein of SARS-CoV-2, Hemagglutinin of Influenza, and the gp120/gp41 complex of HIV-1.

Other names

Envelope glycoproteinSpike proteinSurface antigenViral attachment proteinFusion proteinPeplomer

Neutralization, Viral entry inhibition, Fusion inhibition, Attachment inhibition