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The Influenza A virus hemagglutinin protein (H5 subtype) mediates both cell binding via sialic acid recognition and subsequent membrane fusion after endocytosis. Its structure—a trimer with distinct head/stem domains—underpins its function as both an essential factor in infectivity and as a key immunogen targeted by vaccines. Variability within its sequence drives antigenic evolution while certain features such as polybasic cleavage sites contribute directly to pathogenicity in highly virulent strains like H5N1.
Neutralization of viral infectivity by blocking receptor binding or membrane fusion; stimulation of antibody production
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