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The **Mumps virus hemagglutinin-neuraminidase glycoprotein** (HN protein) is a multifunctional viral surface glycoprotein essential for mumps virus infectivity. It is a type II membrane protein, consisting of 582 amino acids, and forms homodimers and tetramers on the viral envelope[3]. The HN protein combines receptor recognition (acting as hemagglutinin) and neuraminidase enzymatic activity. It attaches the virus to host cell surface receptors by binding to α2,3-linked sialic acid residues on glycoconjugates[6][3][9]. After receptor engagement, HN protein facilitates the activation of the fusion (F) protein, enabling fusion between viral and host cell membranes and viral entry[5][3][9]. Its neuraminidase activity cleaves sialic acid from cellular and viral glycoproteins, a step crucial for viral particle release and prevention of virus self-aggregation[5][1][3]. HN is a key determinant of tissue tropism, immune evasion, and neurovirulence in both wild-type and vaccine strains[7][9], making it a prominent target for mumps antiviral development and a marker of viral pathogenesis and vaccine safety.
Drugs would act as neuraminidase inhibitors (blocking the enzymatic cleavage needed for viral release and spread)[5][1]
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