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Hemagglutinin of Influenza A H1N1 virus is a trimeric, class I fusion glycoprotein displayed on the viral surface, essential for viral infectivity[1][3][4][5]. Each monomer consists of two subunits (HA1 and HA2) generated after proteolytic cleavage of a precursor (HA0); HA1 forms the globular head responsible for binding to sialic acid receptors on host cells, while HA2 forms the stalk region critical for fusion of viral and host cell membranes[1][2][5][6]. Hemagglutinin is the principal target of neutralizing antibodies and thus a central antigenic component of influenza vaccines[3][5]. The protein’s high variability, especially in its head domain, enables immune evasion and is the basis for seasonal influenza epidemics and occasional pandemics, such as the 2009 H1N1 outbreak[1][5]. Immunity to HA, as measured by hemagglutination inhibition assays, is considered the best correlate of protection for influenza vaccines[3][5].
Neutralizing antibodies prevent receptor binding by blocking HA head domain Neutralizing antibodies inhibit membrane fusion by binding HA stalk domain Vaccines induce immune response against HA to confer protective immunity
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