Measles virus fusion protein, hemagglutinin, and nucleoprotein (MeV F, H, and N)

The **measles virus fusion protein (F)**, **hemagglutinin (H)**, and **nucleoprotein (N)** are three essential proteins encoded by the measles virus, a member of the Paramyxoviridae family. The **hemagglutinin (H) protein** is a viral glycoprotein that mediates attachment to host cell receptors, including SLAMF1 (CD150), Nectin-4 (PVRL4), and sometimes CD46, determining key aspects of cell tropism and initiating viral entry[4][7]. Upon H binding to a cellular receptor, the **fusion (F) protein**, a class I viral fusion glycoprotein, is triggered to mediate the merger of the viral envelope with the host membrane, enabling viral genome entry and, in some cases, syncytia formation (cell-cell fusion)[1][2][4]. The **nucleoprotein (N)** encapsidates the viral RNA and, together with the phosphoprotein (P) and RNA-dependent RNA polymerase (L), forms the ribonucleoprotein complex, critical for RNA synthesis and genome protection[4][5][10]. All three proteins are core immunological targets for vaccine design and serodiagnostics, and could theoretically be targeted by antiviral drugs or neutralizing antibodies[6][7]. While no direct-acting small molecule inhibitors are currently licensed, neutralizing antibodies against H or F are a focus of research. Safety concerns are inherent to live vaccine strains (attenuation, neurovirulence), but these proteins themselves constitute well-established, clinically validated targets[6][7].

Other names

MeV F proteinMeV H proteinMeV N proteinFusion protein (F)Hemagglutinin (H)Nucleoprotein (N)

For fusion/entry inhibitors: block F-mediated membrane fusion, or H-mediated receptor attachment. For neutralizing antibodies: bind to H or F to prevent viral entry