Measles morbillivirus hemagglutinin and fusion proteins (MeV H/F)

The Measles morbillivirus hemagglutinin (H) and fusion (F) proteins are the primary surface glycoproteins that mediate viral entry into host cells. The H protein is a type II transmembrane protein that functions as the attachment protein, binding to host receptors such as signaling lymphocytic activation molecule (SLAM/CD150) on immune cells and nectin-4 on epithelial cells [Creative Diagnostics, 2024; NIH, 2016]. Upon receptor binding, H undergoes conformational changes that trigger the F protein, a type I transmembrane protein, to transition from a metastable prefusion state to a stable postfusion state [MDPI, 2016; NIH, 2021]. This structural rearrangement facilitates the fusion of the viral envelope with the host cell membrane, allowing the viral ribonucleocapsid to enter the cytoplasm [Creative Diagnostics, 2024; NIH, 2016]. These proteins are essential for the formation of syncytia, a hallmark of measles pathology characterized by multinucleated giant cells [Wikipedia, 2024; NIH, 2021]. They are the primary targets for neutralizing antibodies and are being investigated as targets for novel entry inhibitors, including small molecules like AS-48 and peptides like the Fusion Inhibitory Peptide (FIP) [NIH, 2021]. Mutations in these proteins, particularly the F protein, are associated with persistent central nervous system infections such as subacute sclerosing panencephalitis (SSPE) [ResearchGate, 2019].

Other names

Measles virus hemagglutinin (H) and fusion (F) proteinsMeV H/F complexViral entry machineryAttachment and fusion glycoproteinsMorbillivirus fusion machinery

Entry inhibition by stabilizing the prefusion conformation of the fusion protein and blocking receptor-mediated triggering of the fusion process [NIH, 2021; MDPI, 2016].