8T1G
The crystal structure of hemagglutinin form a h7n9 influenza virus (a/shanghai/1/2013) in complex with antibody 1E11
Summary for 8T1G
| Entry DOI | 10.2210/pdb8t1g/pdb |
| Descriptor | Hemagglutinin HA1, Hemagglutinin HA2, 1E11 Fab Heavy chain, ... (9 entities in total) |
| Functional Keywords | hemagglutinin, influenza, virus, antibody, h7n9, immune system, immune system-viral protein complex, immune system/viral protein |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 12 |
| Total formula weight | 328821.91 |
| Authors | Zhou, T.,Kwong, P.D. (deposition date: 2023-06-02, release date: 2024-05-29, Last modification date: 2025-04-02) |
| Primary citation | Mantus, G.E.,Cerutti, G.,Chambers, M.,Gillespie, R.A.,Shimberg, G.D.,Spangler, A.,Gorman, J.,Zhou, T.,Shen, C.H.,Kanekiyo, M.,Kwong, P.D.,Shapiro, L.,Andrews, S.F. Distinct binding modes drive the broad neutralization profile of two persistent influenza hemagglutinin stem-specific antibody lineages. Structure, 2025 Cited by PubMed Abstract: Elicitation of antibodies to the influenza hemagglutinin stem is a critical part of universal influenza vaccine strategies. While numerous broadly reactive stem antibodies have been isolated, our understanding of how these antibodies mature within the human B cell repertoire is limited. Here, we isolated and tracked two stem-specific antibody lineages over a decade in a single participant that received multiple seasonal and pandemic influenza vaccinations. Despite similar binding and neutralization profiles, antibodies from these lineages utilized fundamentally different interactions to engage the central epitope on the influenza stem. Structural analysis of an unmutated common ancestor from one lineage identified critical residues that were the main drivers of increased affinity and breadth to group 1 influenza subtypes. These observations demonstrate the heterogeneous pathways by which stem-specific antibodies can mature within the human B cell repertoire. PubMed: 40112805DOI: 10.1016/j.str.2025.02.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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