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Hemagglutinin is a homotrimeric glycoprotein located on the surface of the influenza A virus. Each monomer of the HA trimer consists of a globular head domain that binds to sialic acid receptors on host cells and a stem (or stalk) domain that facilitates fusion of the viral envelope with the host cell membrane after endocytosis. The H3N2 subtype of hemagglutinin has been responsible for widespread seasonal influenza outbreaks in humans since 1968. HA is essential for viral entry and is the principal target of neutralizing antibodies elicited by natural infection or vaccination. Its antigenic sites overlap with the receptor-binding site, making it prone to antigenic drift—a major driver of immune escape and the need for continuous vaccine updates[1][2][3][4][6][7].
Neutralizing antibodies block receptor binding or membrane fusion steps Entry inhibitors prevent conformational changes required for fusion
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