Mumps virus Hemagglutinin-neuraminidase and Fusion glycoproteins (MuV HN and F proteins)

The Mumps virus (MuV) surface glycoproteins, Hemagglutinin-neuraminidase (HN) and Fusion (F) protein, are essential for the viral life cycle and serve as the primary targets for the host immune system. The HN protein facilitates viral attachment by binding to sialic acid-containing receptors on host cells and possesses neuraminidase activity that prevents the aggregation of progeny virions during budding. Upon receptor binding, HN triggers a conformational change in the F protein, which mediates the fusion of the viral envelope with the host cell membrane, allowing the viral genome to enter the cytoplasm. These glycoproteins are the key components of live-attenuated vaccines, such as the Jeryl Lynn strain used in the MMR vaccine, which elicit neutralizing antibodies to prevent infection. However, recent outbreaks in vaccinated populations have highlighted challenges such as waning immunity and antigenic differences between vaccine strains and circulating wild-type genotypes. Consequently, these proteins are the focus of research into next-generation subunit vaccines and monoclonal antibody therapies designed to provide broader and more durable protection.

Other names

Mumps virus surface proteinsHN proteinF proteinMuV-HNMuV-FHemagglutinin-neuraminidaseFusion glycoprotein F0

Induction of neutralizing antibodies that block viral attachment and membrane fusion; inhibition of viral entry into host cells.