9NRT
Crystal structure of the H5 influenza virus hemagglutinin from A/duck/France/161108h/2016 (H5N8) clade 2.3.4.4b in complex with O-linked glycan 25
Summary for 9NRT
| Entry DOI | 10.2210/pdb9nrt/pdb |
| Descriptor | Hemagglutinin HA1 chain, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose, ... (15 entities in total) |
| Functional Keywords | h5 hemagglutinin, clade 2.3.4.4b, o-linked glycan, receptor specificity, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 10 |
| Total formula weight | 187962.61 |
| Authors | Zhu, X.,Wilson, I.A. (deposition date: 2025-03-14, release date: 2026-01-14, Last modification date: 2026-01-28) |
| Primary citation | Weber, J.,Ponse, N.L.D.,Zhu, X.,Carrasco, M.R.,Han, A.X.,Funk, M.,Lin, T.H.,Garcia, A.G.,Spruit, C.M.,Zhang, D.,Yu, W.,Wilson, I.A.,Richard, M.,Boons, G.J.,de Vries, R.P. The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans. Plos Pathog., 22:e1013812-e1013812, 2026 Cited by PubMed Abstract: Highly pathogenic H5Ny influenza A viruses are causing unprecedented, season-independent outbreaks across avian and mammalian species, including dairy cattle, a novel reservoir. The sialoside-binding properties of influenza A hemagglutinin (HA) are strongly related to its ability to infect and transmit between hosts. Mucin-like O-glycans, omnipresent in respiratory tracts, have been understudied as viral receptors due to their complexity. To address this, we synthesized 25 O-linked glycans with diverse sialosides, including modifications by fucosides and sulfates. Our findings reveal that H5Ny 2.3.4.4b viruses bind core 3 sialyl-Lewisx and Sia-Gal-β3GalNAc, O-linked glycans not recognized by classical H5 or other avian viruses. By determining crystal structures, we resolved the structural features of four glycans in an H5 hemagglutinin (HA) from a 2016 2.3.4.4b virus. While these viruses do not bind human-type receptors, their broad receptor specificity enhances binding to human tracheal tissues, suggesting that O-glycan recognition could contribute to the continues spillover of this clade. PubMed: 41557749DOI: 10.1371/journal.ppat.1013812 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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