3UBN

Influenza hemagglutinin from the 2009 pandemic in complex with ligand 6SLN

Summary for 3UBN

• Entry DOI: 10.2210/pdb3ubn/pdb
• Related: 3UBE 3UBJ 3UBQ
• Related PRD ID: PRD_900046
• Descriptor: Hemagglutinin HA1, Hemagglutinin HA2, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: viral envelope protein, hemagglutinin, viral fusion protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Influenza A virus; More
• Total number of polymer chains: 12
• Total formula weight: 347141.69

Authors

Xu, R.,Wilson, I.A. (deposition date: 2011-10-24, release date: 2011-11-23, Last modification date: 2024-10-09)

Primary citation

Xu, R.,McBride, R.,Nycholat, C.M.,Paulson, J.C.,Wilson, I.A.
Structural Characterization of the Hemagglutinin Receptor Specificity from the 2009 H1N1 Influenza Pandemic.
J.Virol., 86:982-990, 2012

PubMed Abstract: Influenza virus 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 20th century, the HA normally has acquired specificity for human-like receptors before widespread infection. Crystal structures of the H1 HA from the 2009 human pandemic (A/California/04/2009 [CA04]) in complex with human and avian receptor analogs reveal conserved recognition of the terminal sialic acid of the glycan ligands. However, favorable interactions beyond the sialic acid are found only for α2-6-linked glycans and are mediated by Asp190 and Asp225, which hydrogen bond with Gal-2 and GlcNAc-3. For α2-3-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 α2-6- and α2-3-linked glycans, now elucidate the structural basis of receptor-binding specificity for H1 HAs in human and avian viruses and provide a structural explanation for the preference for α2-6 siaylated glycan receptors for the 2009 pandemic swine flu virus.

PubMed: 22072785
DOI: 10.1128/JVI.06322-11

Experimental method

X-RAY DIFFRACTION (2.5079 Å)