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Publication Abstract from PubMed

Influenza hemagglutinin (HA) is the viral envelope protein that mediates viral attachment to host cells and elicits membrane fusion. The HA receptor-binding specificity is a key determinant for the host range and transmissibility of influenza viruses. In human pandemics of the 20(th) century, the HA has normally acquired specificity for human-like receptors before widespread infection. Crystal structures of the H1 HA from the 2009 human pandemic (CA04, A/California/04/2009) in complex with human and avian receptor analogs reveals conserved recognition of the terminal sialic acid of the glycan ligands. However, favorable interactions beyond the sialic acid are found only for alpha2-6-linked glycans and are mediated by Asp190 and Asp225, which hydrogen bond with Gal-2 and GlcNAc-3. For alpha2-3-linked glycan receptors, no specific interactions beyond the terminal sialic acid are observed. Our structural and glycan microarray analyses, in the context of other high resolution HA structures with alpha2-6 and alpha2-3-linked glycans, now elucidate the structural basis of receptor binding specificity for H1 HAs in human and avian viruses and provide an structural explanation for the preference for alpha2-6 siaylated glycan receptors for the 2009 pandemic swine flu virus.

Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic.,Xu R, McBride R, Nycholat CM, Paulson JC, Wilson IA J Virol. 2011 Nov 9. PMID:22072785^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.