8IB1
Structure of the LAH31 Fab bound to an influenza virus HA epitope peptide
Summary for 8IB1
| Entry DOI | 10.2210/pdb8ib1/pdb |
| Descriptor | LAH31 Fab light chain, LAH31 Fab heavy chain, Hemagglutinin HA2 chain, ... (4 entities in total) |
| Functional Keywords | antibody, fab, influenza, epitope, antiviral protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 56894.18 |
| Authors | Suzuki, T.,Hashiguchi, T. (deposition date: 2023-02-09, release date: 2023-07-26, Last modification date: 2024-10-16) |
| Primary citation | Tonouchi, K.,Adachi, Y.,Suzuki, T.,Kuroda, D.,Nishiyama, A.,Yumoto, K.,Takeyama, H.,Suzuki, T.,Hashiguchi, T.,Takahashi, Y. Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope. Plos Pathog., 19:e1011554-e1011554, 2023 Cited by PubMed Abstract: Plasticity of influenza virus hemagglutinin (HA) conformation increases an opportunity to generate conserved non-native epitopes with unknown functionality. Here, we have performed an in-depth analysis of human monoclonal antibodies against a stem-helix region that is occluded in native prefusion yet exposed in postfusion HA. A stem-helix antibody, LAH31, provided IgG Fc-dependent cross-group protection by targeting a stem-helix kinked loop epitope, with a unique structure emerging in the postfusion state. The structural analysis and molecular modeling revealed key contact sites responsible for the epitope specificity and cross-group breadth that relies on somatically mutated light chain. LAH31 was inaccessible to the native prefusion HA expressed on cell surface; however, it bound to the HA structure present on infected cells with functional linkage to the Fc-mediated clearance. Our study uncovers a novel non-native epitope that emerges in the postfusion HA state, highlighting the utility of this epitope for a broadly protective antigen design. PubMed: 37556494DOI: 10.1371/journal.ppat.1011554 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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