Hemagglutinin H7 protein (HA H7 or H7 HA)

Hemagglutinin H7 protein is a trimeric, integral membrane glycoprotein located on the surface of Influenza A virions[5][4]. Comprised of HA1 and HA2 subunits, it binds to sialic acid receptors on host epithelial cells, enabling viral attachment. Upon endocytosis, acidification triggers dramatic structural rearrangements in HA, exposing a fusion peptide that merges viral and host membranes for genome entry[5][4]. The H7 subtype belongs to a distinct phylogenetic clade among the 16 known influenza hemagglutinin types[2]. Structurally, H7 shares features with other class I viral fusion proteins but exhibits specific antigenic and conformational properties, driving its selection as a target for neutralizing antibodies and fusion inhibitors[1][2][3][6]. Safety concerns arise from frequent mutations, zoonotic transmission risks, and challenges in vaccine coverage.

Other names

H7 hemagglutininHA H7Influenza A hemagglutinin subtype H7

Inhibition of conformational changes required for membrane fusion (e.g., TBHQ stabilizes HA trimer to block fusion); Neutralization by monoclonal antibodies that bind specific epitopes and destabilize HA structure, blocking viral entry