6Q1Z
Crystal structure of human 1G04 Fab in complex with influenza virus neuraminidase from A/Hunan/02650/2016 (H7N9)
Summary for 6Q1Z
| Entry DOI | 10.2210/pdb6q1z/pdb |
| Descriptor | Neuraminidase, 1G04 Fab kappa light chain, 1G04 Fab IgG1 heavy chain, ... (7 entities in total) |
| Functional Keywords | broadly protective human antibody, neuraminidase, inhibition, active site, antibody-neuraminidase complex, viral protein, hydrolase-immune system complex, hydrolase/immune system |
| Biological source | Influenza A virus More |
| Total number of polymer chains | 6 |
| Total formula weight | 192775.46 |
| Authors | Zhu, X.,Wilson, I.A. (deposition date: 2019-08-06, release date: 2019-10-23, Last modification date: 2024-11-06) |
| Primary citation | Stadlbauer, D.,Zhu, X.,McMahon, M.,Turner, J.S.,Wohlbold, T.J.,Schmitz, A.J.,Strohmeier, S.,Yu, W.,Nachbagauer, R.,Mudd, P.A.,Wilson, I.A.,Ellebedy, A.H.,Krammer, F. Broadly protective human antibodies that target the active site of influenza virus neuraminidase. Science, 366:499-504, 2019 Cited by PubMed Abstract: Better vaccines against influenza virus are urgently needed to provide broader protection against diverse strains, subtypes, and types. Such efforts are assisted by the identification of novel broadly neutralizing epitopes targeted by protective antibodies. Influenza vaccine development has largely focused on the hemagglutinin, but the other major surface antigen, the neuraminidase, has reemerged as a potential target for universal vaccines. We describe three human monoclonal antibodies isolated from an H3N2-infected donor that bind with exceptional breadth to multiple different influenza A and B virus neuraminidases. These antibodies neutralize the virus, mediate effector functions, are broadly protective in vivo, and inhibit neuraminidase activity by directly binding to the active site. Structural and functional characterization of these antibodies will inform the development of neuraminidase-based universal vaccines against influenza virus. PubMed: 31649200DOI: 10.1126/science.aay0678 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.446 Å) |
Structure validation
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