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Influenza A virus H1N1 hemagglutinin (HA) is a homotrimeric glycoprotein on the viral envelope, synthesized as an inactive precursor HA0 that is cleaved into HA1 and HA2 subunits by host proteases for activation. HA1 forms the globular head containing the receptor binding domain (RBD) that attaches to sialic acid on host cells, while HA2 forms the stalk responsible for low pH-induced conformational changes enabling viral-host membrane fusion in the endosome. The structure includes conserved sialic acid binding residues and antigenic sites prone to variation, influencing vaccine and antibody efficacy.[1][2][5][6]
Neutralization of receptor binding domain (head), Inhibition of membrane fusion (stalk-targeting antibodies)
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