Structural highlights
FunctionC7S226_I57A0 Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643] Publication Abstract from PubMedWe report structural characterization of the first antibody identified to cross-neutralize multiple subtypes of influenza A viruses. The crystal structure of mouse antibody C179 bound to the pandemic 1957 H2N2 hemagglutinin (HA) reveals that it targets a similar epitope on the HA stem as the recently identified human broadly neutralizing antibodies (bnAbs). C179 also inhibits the low-pH conformational change of the HA, but uses a different angle of approach and both heavy and light chains. Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 hemagglutinin.,Dreyfus C, Ekiert DC, Wilson IA J Virol. 2013 Apr 3. PMID:23552413[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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