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The Measles virus envelope glycoproteins, comprising the Hemagglutinin (H) and Fusion (F) proteins, are critical components of the Measles morbillivirus virion. The H protein (UniProt P08362) is responsible for recognizing and binding to specific host cell receptors, including signaling lymphocytic activation molecule (SLAM/CD150) and Nectin-4, which determines the virus's tissue tropism. Following attachment, the F protein (UniProt P03372) undergoes a conformational change that triggers the fusion of the viral envelope with the host cell plasma membrane, allowing the viral genome to enter the cytoplasm. These glycoproteins are the primary targets for the host's neutralizing antibody response and are the basis for the highly effective live-attenuated measles vaccine (StatPearls: Measles). In therapeutic development, they are targeted by small-molecule inhibitors and monoclonal antibodies designed to block viral entry and prevent the formation of syncytia, which is a hallmark of measles infection (PubMed: 21123656, 24740835).
Neutralization of viral particles to prevent host cell attachment and inhibition of the membrane fusion process required for viral entry.
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