Measles morbillivirus hemagglutinin and fusion glycoproteins (MeV H and F)

The Measles morbillivirus envelope glycoproteins, Hemagglutinin (H) and Fusion (F), are the primary mediators of viral entry into host cells. The H protein is a type II transmembrane glycoprotein that functions as the attachment protein, recognizing and binding to specific host receptors such as signaling lymphocytic activation molecule (SLAM/CD150) on immune cells and Nectin-4 on epithelial cells (UniProt P08362). Upon receptor binding, the H protein undergoes a conformational change that is transmitted to the F protein, a type I transmembrane glycoprotein (UniProt P03372). This trigger causes the F protein to transition from a metastable pre-fusion state to a stable post-fusion state, inserting a fusion peptide into the host cell membrane and facilitating the merger of the viral and cellular membranes (Plemper et al., 2011). These glycoproteins are the principal targets of the host's neutralizing antibody response and are the key antigenic components of the live-attenuated measles vaccine. In addition to their role in primary infection, mutations in these proteins are associated with the development of subacute sclerosing panencephalitis (SSPE), a fatal neurodegenerative disease (Navaratnarajah et al., 2016). Therapeutic strategies targeting H and F include the use of neutralizing antibodies for post-exposure prophylaxis and the development of small-molecule fusion inhibitors like AS-48. Understanding the structural dynamics of the H-F complex is crucial for designing next-generation antivirals that can block viral entry and prevent the spread of measles.

Other names

Measles virus H and F proteinsMeV envelope glycoproteinsHemagglutinin (H) proteinFusion (F) proteinAttachment and fusion proteins

The H protein binds to host receptors (CD150/SLAM or Nectin-4), which triggers the F protein to undergo a conformational change, leading to the fusion of the viral envelope with the host cell membrane and subsequent viral entry (Navaratnarajah et al., 2016).