9DIQ
Crystal structure of Apo-H5 hemagglutinin from the influenza virus A/Texas/37/2024 (H5N1)
Summary for 9DIQ
| Entry DOI | 10.2210/pdb9diq/pdb |
| Descriptor | Hemagglutinin HA1, Hemagglutinin HA2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | h1n1, antibody, hemagglutinin, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 12 |
| Total formula weight | 343579.99 |
| Authors | Lin, T.H.,Zhu, Y.,Wilson, I.A. (deposition date: 2024-09-05, release date: 2024-12-04, Last modification date: 2025-01-22) |
| Primary citation | Lin, T.H.,Zhu, X.,Wang, S.,Zhang, D.,McBride, R.,Yu, W.,Babarinde, S.,Paulson, J.C.,Wilson, I.A. A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors. Science, 386:1128-1134, 2024 Cited by PubMed Abstract: In 2024, several human infections with highly pathogenic clade 2.3.4.4b bovine influenza H5N1 viruses in the United States raised concerns about their capability for bovine-to-human or even human-to-human transmission. In this study, analysis of the hemagglutinin (HA) from the first-reported human-infecting bovine H5N1 virus (A/Texas/37/2024, Texas) revealed avian-type receptor binding preference. Notably, a GlnLeu substitution switched Texas HA binding specificity to human-type receptors, which was enhanced when combined with an AsnLys mutation. Crystal structures of the Texas HA with avian receptor analog LSTa and its GlnLeu mutant with human receptor analog LSTc elucidated the structural basis for this preferential receptor recognition. These findings highlight the need for continuous surveillance of emerging mutations in avian and bovine clade 2.3.4.4b H5N1 viruses. PubMed: 39636969DOI: 10.1126/science.adt0180 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.69 Å) |
Structure validation
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