Measles virus fusion glycoprotein (MeV-F)

The Measles virus fusion glycoprotein (F protein) is a critical type I transmembrane protein located on the viral envelope, essential for mediating viral entry into host cells. It is synthesized as an inactive precursor, F0, which must be proteolytically cleaved by host cell proteases into disulfide-linked F1 and F2 subunits to become biologically active (UniProt: P03372). The F protein functions in a metastable pre-fusion state and is triggered to undergo a massive, irreversible conformational change when the associated hemagglutinin (H) protein binds to host receptors such as CD150 (SLAM) or nectin-4 (PubMed: 21835787). This conformational shift drives the insertion of a fusion peptide into the host membrane, facilitating the merger of viral and cellular membranes or the formation of multinucleated giant cells known as syncytia (PubMed: 25505233). As a primary target for the host's neutralizing antibody response, the F protein is the central component of current measles vaccines and a major focus for the development of small-molecule fusion inhibitors (PubMed: 30643119). These therapeutic candidates, such as ERDRP-0519, typically bind to a hydrophobic pocket within the F protein stalk, stabilizing the pre-fusion conformation and effectively blocking viral infection (PubMed: 22114335).

Other names

Fusion proteinF proteinMeasles virus F proteinProtein F

Inhibition of the conformational transition of the F protein from its metastable pre-fusion state to the highly stable post-fusion state, which prevents the merger of the viral envelope with the host cell membrane.