Mumps orthorubulavirus hemagglutinin-neuraminidase and fusion glycoproteins (MuV HN and F)

Mumps orthorubulavirus glycoproteins HN (hemagglutinin-neuraminidase) and F (fusion) are the two essential surface proteins that mediate the entry of the mumps virus into host cells (UniProt: P06941, P06940). The HN protein is responsible for recognizing and binding to sialic acid receptors on the surface of target cells, while also possessing neuraminidase activity that prevents viral self-aggregation by cleaving sialic acid from progeny virions (PubMed: 19372065). Following attachment, the F protein undergoes a major conformational change, triggered by the HN-receptor interaction, which facilitates the fusion of the viral envelope with the host cell plasma membrane. These glycoproteins are the primary targets for neutralizing antibodies, making them the central components for vaccine development and immune protection. The widely used MMR (measles, mumps, and rubella) vaccine utilizes live-attenuated mumps virus to elicit a robust immune response against these proteins (CDC, 2021). Understanding the structure and function of the HN and F complex is crucial for monitoring antigenic drift and developing potential antiviral therapies, such as fusion inhibitors, to combat mumps outbreaks.

Other names

Mumps virus HN and F proteinsHemagglutinin-neuraminidaseFusion proteinMuV surface glycoproteinsMumps virus attachment and fusion proteins

Vaccines induce the production of neutralizing antibodies that bind to the HN protein to block viral attachment to host cells and to the F protein to prevent membrane fusion and subsequent viral entry (CDC, 2021; PubMed: 22090119).