9NJ2
N1 neuraminidase of influenza A/Vietnam/1203/2004 H5N1 in complex with four FNI9 Fab molecules
Summary for 9NJ2
| Entry DOI | 10.2210/pdb9nj2/pdb |
| EMDB information | 49462 |
| Descriptor | Neuraminidase, FNI9 Fab heavy chain, FNI9 Fab light chain, ... (5 entities in total) |
| Functional Keywords | antibody, neuraminidase, n1, h5n1, influenza, neutralizing antibody, viral protein-immune system complex, viral protein/immune system |
| Biological source | Influenza A virus (A/Viet Nam/1203/2004(H5N1)) More |
| Total number of polymer chains | 12 |
| Total formula weight | 312714.02 |
| Authors | Errico, J.M.,Dang, H.V.,Snell, G. (deposition date: 2025-02-26, release date: 2026-03-11, Last modification date: 2026-04-22) |
| Primary citation | Moriyama, S.,di Iulio, J.,Zatta, F.,Hauser, K.,Asanuma, H.,Munoz, H.E.,Errico, J.M.,Adachi, Y.,Dang, H.V.,Czudnochowski, N.,Sasaki, E.,Chen, A.,Chen, Y.P.,Kotaki, R.,Peter, A.,Vetti, E.,Onodera, T.,Cyrus Maher, M.,Rosen, L.E.,Shirakura, M.,Snell, G.,Hasegawa, H.,Takahashi, Y.,Corti, D.,Pizzuto, M.S. Potent efficacy of an NA-targeting antibody against a broad spectrum of H5N1 influenza viruses. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: For nearly 30 years, Goose/Guangdong-derived highly pathogenic avian influenza H5N1 viruses have posed significant risks to economic stability, food security, and public health. Virus evolution has resulted in various clades, including the panzootic subclade 2.3.4.4b, recognized for its pandemic potential. Here we present the potent in vitro activity of FNI9, a pan-influenza NA-inhibiting monoclonal antibody, against a range of pseudoparticles with NA spanning decades of H5N1 virus evolution. FNI9 also shows strong prophylactic protection in female mice against lethal challenges with H5N1 from clade 1 and 2.3.4.4b. Cryo-EM and molecular dynamics analysis reveal that FNI9 binds to 7 highly conserved H5N1 NA residues (R118, E119, D151, E228, E278, R293, and R368). In silico evolutionary escape profiling and machine learning predict low escapability, high fitness costs, and minimal spread likelihood for viral mutations that evade FNI9 binding. These findings support FNI9 broad protection and underscore the NA role in future influenza vaccine design. PubMed: 41771877DOI: 10.1038/s41467-026-70036-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.4 Å) |
Structure validation
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