Influenza A virus H10N8 hemagglutinin (HA or H10N8 HA)

Influenza A virus H10N8 hemagglutinin is a trimeric surface glycoprotein that serves as the primary attachment and membrane fusion factor for viral entry into host cells.[1][2][3] The protein functions as a class I fusion protein with a globular head domain responsible for binding sialic acid receptors on host cell surfaces and a stem domain containing the membrane fusion machinery.[1][4] H10N8 preferentially recognizes α2,3-linked sialic acid receptors characteristic of avian cells, distinguishing it from human-adapted influenza strains.[2][4] As the most abundant glycoprotein on the influenza virion surface, hemagglutinin is the major antigen targeted by the host immune system and serves as the primary target for vaccine development and therapeutic antibody design.[1][2] H10N8 is classified as an emerging zoonotic subtype with pandemic potential; while naturally circulating strains currently lack the mutations necessary for efficient human-to-human transmission, the protein's capacity for antigenic evolution poses ongoing surveillance and public health concerns.[1][2] Therapeutic strategies targeting H10N8 hemagglutinin include traditional neutralizing antibodies, broadly neutralizing antibodies targeting conserved stem epitopes, and antiviral compounds that inhibit the conformational changes required for membrane fusion.

Other names

Hemagglutinin (HA)H10 hemagglutininHA subtype H10Surface glycoproteinAttachment protein

Therapeutic strategies targeting H10N8 hemagglutinin include traditional neutralizing antibodies, broadly neutralizing antibodies targeting conserved stem epitopes, and antiviral compounds that inhibit the conformational changes required for membrane fusion.