9DRU
Crystal structure of 04709_4F04 Fab in complex with H1 HA from A/California/04/2009(H1N1)
Summary for 9DRU
| Entry DOI | 10.2210/pdb9dru/pdb |
| Descriptor | Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 04709_4F04, heavy chain, ... (6 entities in total) |
| Functional Keywords | h1n1, antibody, hemagglutinin, viral protein-immune system complex, viral protein/immune system |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 4 |
| Total formula weight | 103766.88 |
| Authors | |
| Primary citation | Lin, T.H.,Lee, C.D.,Fernandez-Quintero, M.L.,Ferguson, J.A.,Han, J.,Zhu, X.,Yu, W.,Guthmiller, J.J.,Krammer, F.,Wilson, P.C.,Ward, A.B.,Wilson, I.A. Structurally convergent antibodies derived from different vaccine strategies target the influenza virus HA anchor epitope with a subset of V H 3 and V K 3 genes. Nat Commun, 16:1268-1268, 2025 Cited by PubMed Abstract: H1N1 influenza viruses are responsible for both seasonal and pandemic influenza. The continual antigenic shift and drift of these viruses highlight the urgent need for a universal influenza vaccine to elicit broadly neutralizing antibodies (bnAbs). Identification and characterization of bnAbs elicited in natural infection and immunization to influenza virus hemagglutinin (HA) can provide insights for development of a universal influenza vaccine. Here, we structurally and biophysically characterize four antibodies that bind to a conserved region on the HA membrane-proximal region known as the anchor epitope. Despite some diversity in their V and V genes, the antibodies interact with the HA through germline-encoded residues in HCDR2 and LCDR3. Somatic mutations on HCDR3 also contribute hydrophobic interactions with the conserved HA epitope. This convergent binding mode provides extensive neutralization breadth against H1N1 viruses and suggests possible countermeasures against H1N1 viruses. PubMed: 39894881DOI: 10.1038/s41467-025-56496-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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