9BDG
Influenza A virus Hemagglutinin H3/Darwin/6/2021 in complex with Fab ADI-85647
Summary for 9BDG
| Entry DOI | 10.2210/pdb9bdg/pdb |
| EMDB information | 44452 |
| Descriptor | Hemagglutinin, Fab ADI-85647 Heavy chain, Ig-like domain-containing protein, ... (9 entities in total) |
| Functional Keywords | hemagglutinin, influenza a, antibody, fab, viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 9 |
| Total formula weight | 331431.26 |
| Authors | Ferreira Ramos, A.S.,Bajic, G. (deposition date: 2024-04-11, release date: 2024-11-13, Last modification date: 2025-05-28) |
| Primary citation | Maurer, D.P.,Vu, M.,Ferreira Ramos, A.S.,Dugan, H.L.,Khalife, P.,Geoghegan, J.C.,Walker, L.M.,Bajic, G.,Schmidt, A.G. Conserved sites on the influenza H1 and H3 hemagglutinin recognized by human antibodies. Sci Adv, 11:eadu9140-eadu9140, 2025 Cited by PubMed Abstract: Monoclonal antibodies (mAbs) targeting the influenza hemagglutinin (HA) can be used as prophylactics or templates for next-generation vaccines. Here, we isolated broad, subtype-neutralizing mAbs from human B cells recognizing the H1 or H3 HA "head" and a mAb engaging the conserved stem. The H1 mAbs bind the lateral patch epitope on HAs from 1933 to 2021 and a prepandemic swine H1N1 virus. We improved neutralization potency using directed evolution toward a contemporary H1 HA. Deep mutational scanning of four antigenically distinct H1N1 viruses identified potential viral escape pathways. For the H3 mAbs, we used cryo-electron microscopy to define their epitopes: One mAb binds the side of the HA head, accommodating the N133 glycan and a pocket underneath the receptor binding site; the other mAb recognizes an HA stem epitope that partially overlaps with previously characterized mAbs but with distinct antibody variable genes. Collectively, these mAbs identify conserved sites recognized by broadly-reactive mAbs that may be elicited by next-generation vaccines. PubMed: 40267182DOI: 10.1126/sciadv.adu9140 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.01 Å) |
Structure validation
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