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The influenza B hemagglutinin (HA) protein is a homotrimeric glycoprotein found on the surface of influenza B viruses. It is essential for viral infectivity, mediating both the initial attachment to host cells and subsequent membrane fusion required for viral entry. The HA protein exists as a trimer, with each monomer composed of two subunits: HA1 and HA2. The globular head contains the receptor-binding site (RBS), which interacts with sialic acid-containing receptors on host cells. Antigenic drift occurs through amino acid substitutions—especially within or near key epitopes—enabling escape from pre-existing immunity.
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