Measles virus fusion protein (MeV-F)

The Measles virus fusion protein (MeV-F) is a critical type I transmembrane glycoprotein located on the surface of the measles virus envelope. It plays a fundamental role in viral pathogenesis by mediating the fusion of the viral envelope with the host cell plasma membrane, a process triggered by the binding of the hemagglutinin (H) protein to host receptors like CD150 or nectin-4 (UniProt, 2023). MeV-F is synthesized as an inactive precursor (F0) that must be proteolytically cleaved into F1 and F2 subunits by host cell proteases to become biologically active (PubMed, 2021). Beyond initial entry, the protein facilitates cell-to-cell fusion, leading to the formation of multinucleated giant cells or syncytia, which is a hallmark of measles infection (StatPearls, 2023). As a primary target for the host immune response, MeV-F is a key component in live-attenuated vaccines, which elicit neutralizing antibodies that prevent viral entry (CDC, 2020). Research into small-molecule fusion inhibitors targeting MeV-F continues to be an area of interest for treating severe cases or complications like subacute sclerosing panencephalitis (SSPE) (Journal of Virology, 2019).

Other names

Fusion glycoproteinF proteinMeasles virus fusion antigenProtein F

The fusion protein mediates the fusion of the viral envelope with the host cell membrane or the fusion of infected cells with adjacent uninfected cells (syncytia formation). Drugs or antibodies targeting this protein typically act as fusion inhibitors, preventing the conformational change required for membrane merging or physically blocking the interaction between the viral and host membranes.