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The Measles virus surface glycoproteins comprise two essential proteins: the Hemagglutinin (H) and the Fusion (F) protein, which work in tandem to mediate viral entry into host cells (UniProt P08362, P03372). The H protein is a type II transmembrane glycoprotein 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 (PubMed: 21885615). Upon receptor binding, the H protein triggers the F protein, a type I transmembrane glycoprotein, to undergo a dramatic conformational change that drives the fusion of the viral envelope with the host plasma membrane (PubMed: 22238302). These glycoproteins are the primary targets of the host's neutralizing antibody response and are the key components of the live-attenuated measles vaccine (NIH: StatPearls). Therapeutic interventions targeting these proteins include experimental small molecules like ERDRP-0519, which inhibits the H protein, and various fusion-inhibitory peptides designed to block viral entry and syncytia formation (PubMed: 25855243).
Neutralization of viral entry by blocking receptor binding (H protein) or preventing the conformational change required for membrane fusion (F protein).
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