9EKF
CryoEM structure of H5N1 A/Texas/37/2024 HA bound to Fab 65C6 and an auto glycan occupying the receptor-binding site
Summary for 9EKF
| Entry DOI | 10.2210/pdb9ekf/pdb |
| EMDB information | 48120 |
| Descriptor | Hemagglutinin, Fab 65C6 Heavy Chain, Fab 65C6 Light Chain, ... (5 entities in total) |
| Functional Keywords | h5n1, antibody, influenza, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 9 |
| Total formula weight | 351013.89 |
| Authors | Morano, N.C.,Shapiro, L.,Kwong, P.D. (deposition date: 2024-12-02, release date: 2024-12-18, Last modification date: 2025-02-19) |
| Primary citation | Morano, N.C.,Guo, Y.,Becker, J.E.,Li, Z.,Yu, J.,Ho, D.D.,Shapiro, L.,Kwong, P.D. Structure of a zoonotic H5N1 hemagglutinin reveals a receptor-binding site occupied by an auto-glycan. Structure, 33:228-233.e3, 2025 Cited by PubMed Abstract: Highly pathogenic avian influenza has spilled into many mammals, most notably cows and poultry, with several dozen human breakthrough infections. Zoonotic crossovers, with hemagglutinins mutated to enhance viral ability to use human α2-6-linked sialic acid receptors versus avian α2-3-linked ones, highlight the pandemic risk. To gain insight into these crossovers, we determined the cryoelectron microscopy (cryo-EM) structure of the hemagglutinin from the zoonotic H5N1 A/Texas/37/2024 strain (clade 2.3.4.4b) in complex with a previously reported neutralizing antibody. Surprisingly, we found that the receptor-binding site of this H5N1 hemagglutinin was already occupied by an α2-3-linked sialic acid and that this glycan emanated from asparagine N169 of a neighboring protomer on hemagglutinin itself. This structure thus highlights recognition by influenza hemagglutinin of an "auto"-α2-3-linked sialic acid from N169, an N-linked glycan conserved in 95% of H5 strains, and adds "auto-glycan recognition," which may play a role in viral dispersal, to the complexities surrounding H5N1 zoonosis. PubMed: 39884273DOI: 10.1016/j.str.2025.01.001 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.68 Å) |
Structure validation
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