Measles morbillivirus surface antigens (MeV-H/F)

Measles morbillivirus surface antigens, primarily the Hemagglutinin (H) and Fusion (F) glycoproteins, are critical components of the viral envelope that facilitate host cell entry and systemic spread (UniProt, 2024; Creative Diagnostics, 2024). The H protein mediates attachment by binding to specific host receptors, including SLAMF1 (CD150) on immune cells and Nectin-4 on epithelial cells, while the F protein undergoes a dramatic conformational change to fuse the viral and host membranes (StatPearls, 2025; PDB-101, 2024). These antigens are the primary targets of the host's neutralizing antibody response and are the basis for the highly effective live-attenuated measles vaccines (Wikipedia, 2024; NIH, 2024). In addition to their role in initial infection, these surface proteins enable the formation of multinucleated giant cells (syncytia), which contributes to the profound, transient immunosuppression known as 'immune amnesia' (StatPearls, 2025; MDPI, 2020). Current therapeutic research focuses on developing subunit vaccines and small-molecule fusion inhibitors that target these glycoproteins to provide safer alternatives for immunocompromised patients and to combat the global resurgence of the virus (Journal of Virology, 2014; Drug Discovery News, 2024).

Other names

Measles virus surface glycoproteinsHemagglutinin (H) proteinFusion (F) proteinMeV-HMeV-FMV-HMV-FMeasles virus envelope proteinsMorbillivirus surface antigens

Neutralization of viral attachment and fusion; Inhibition of the F protein conformational change from pre-fusion to post-fusion state.