Mumps virus surface glycoproteins (MuV HN/F)

The mumps virus surface glycoproteins consist of two primary components: the hemagglutinin-neuraminidase (HN) protein and the fusion (F) protein [UniProt P08492, P0DPA4]. The HN protein is responsible for recognizing and binding to sialic acid receptors on the surface of host cells, while also possessing neuraminidase activity to facilitate the release of progeny virions [PubMed: 25140513]. The F protein mediates the fusion of the viral envelope with the host cell membrane, a process triggered by the binding of HN to its receptor [PubMed: 16439524]. These glycoproteins are the primary targets for the host immune system, particularly for the production of neutralizing antibodies [CDC]. Current preventative strategies rely on live-attenuated vaccines, such as the Jeryl Lynn strain, which elicit long-lasting immunity against these surface proteins [StatPearls: NBK534859]. While there are no widely approved antiviral drugs specifically targeting these glycoproteins, they remain the focus of research for developing entry inhibitors, such as the small molecule ERDRP-0519, and improved vaccine formulations to combat outbreaks in vaccinated populations [PubMed: 24848259].

Other names

Hemagglutinin-neuraminidaseFusion proteinMuV surface proteinsHN proteinF proteinMumps virus envelope glycoproteins

Vaccines induce neutralizing antibodies that bind to the HN and F glycoproteins, preventing viral attachment to host sialic acid receptors and inhibiting membrane fusion, thereby neutralizing the virus's ability to infect cells [CDC, PubMed: 16439524].