Mumps virus hemagglutinin-neuraminidase (MuV-HN)

The Mumps virus hemagglutinin-neuraminidase (MuV-HN) is a multifunctional surface glycoprotein essential for the life cycle of the mumps virus, a member of the Paramyxoviridae family. It mediates the initial attachment of the virus to host cells by specifically recognizing and binding to sialic acid-containing glycan receptors, particularly trisaccharides like Neu5Acα2-3Galβ1-4Glc (3'-sialyllactose). Beyond attachment, MuV-HN triggers the fusion protein (F) to facilitate viral entry and possesses neuraminidase activity that cleaves sialic acid residues from progeny virions and host cell surfaces to prevent viral aggregation and promote efficient egress. As a primary target for the host immune response and a critical factor in viral pathogenesis, MuV-HN is a focal point for the development of antiviral therapeutics and is the key component in live-attenuated vaccines. Inhibiting the HN-sialic acid interaction or the protein's enzymatic activity represents a viable strategy for treating mumps-related complications such as orchitis and meningitis.

Other names

HN proteinHemagglutinin-neuraminidase glycoproteinMumps virus HNSialic acid-binding protein

Inhibition of viral attachment to host cells by blocking the sialic acid binding site or inhibiting neuraminidase activity to prevent viral release and spread.