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The Hemagglutinin protein of influenza A virus subtype H10N8 is a homotrimeric integral membrane glycoprotein that functions as both an attachment factor and class I fusion protein. It binds sialic acid-containing receptors on host cells via its globular head domain (comprising receptor-binding domain, vestigial esterase domain), enabling viral attachment, and mediates low-pH-induced membrane fusion through its stem domain (fusion peptide, ectodomain, transmembrane anchor) for viral entry. Synthesized as inactive HA0 precursor, it is cleaved into HA1 (head) and HA2 (stem) subunits linked by disulfide bonds. H10N8 subtype HA contributes to host specificity and is a key target for neutralizing antibodies and vaccines, with structural conservation in the stalk but variability in the head.
Neutralization by binding receptor-binding domain (RBD) to block sialic acid attachment, Inhibition of conformational change in stalk to prevent membrane fusion
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