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The Mumps virus surface proteins, primarily the Hemagglutinin-neuraminidase (HN) and the Fusion (F) protein, are critical components of the viral envelope that facilitate infection (UniProt P08492, P0DPA7). The HN protein mediates the initial attachment of the virus to sialic acid-containing receptors on the host cell surface and possesses neuraminidase activity to facilitate progeny release (PubMed: 26044301). Following attachment, the F protein undergoes a conformational change to trigger the fusion of the viral envelope with the host cell plasma membrane, allowing the viral genome to enter the cytoplasm (PubMed: 23152528). These glycoproteins are the primary targets for the host immune system, particularly for the production of neutralizing antibodies (CDC: Mumps Vaccination). Current therapeutic strategies focus almost exclusively on preventative vaccination using live-attenuated virus strains, such as the Jeryl Lynn strain, which induce long-lasting immunity against these surface antigens. While there are no widely approved small-molecule antivirals specifically targeting these proteins, they remain the focus of research for developing novel entry inhibitors and improved diagnostic assays.
Induction of neutralizing antibodies that block viral attachment and membrane fusion, thereby preventing viral entry into host cells.
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