Mumps virus hemagglutinin-neuraminidase (HN) protein (MuV-HN)

The Mumps virus hemagglutinin-neuraminidase (HN) protein is a multifunctional surface glycoprotein essential for the viral life cycle. It mediates the initial attachment of the virus to host cells by specifically recognizing and binding to α2,3-linked sialic acid-bearing receptors, such as 3'-sialyllactose, sialyl Lewis X, and GM2 gangliosides (Kubota et al., 2016; Kubota et al., 2019). Beyond attachment, the HN protein triggers a conformational change in the adjacent fusion (F) protein to facilitate membrane fusion and viral entry (UniProt P19762). It also possesses neuraminidase (sialidase) activity, which cleaves sialic acid residues from host receptors and progeny virions to prevent viral self-agglutination and promote the release of new viral particles (Forgione et al., 2021). While there are currently no approved antiviral drugs specifically targeting MuV-HN, it remains a primary target for vaccine-induced neutralizing antibodies and the development of novel entry inhibitors (Medscape, 2025). The protein's role in determining tissue tropism and its susceptibility to antigenic drift are critical factors in mumps pathogenesis and vaccine efficacy (NIH, 2022).

Other names

MuV-HNHemagglutinin-neuraminidaseHN proteinMumps virus attachment proteinMumps virus sialidaseMumps virus glycoprotein

Viral attachment inhibition, neuraminidase inhibition, fusion activation inhibition, and neutralization by vaccine-induced antibodies.