9BOP
A broadly-neutralizing antibody against Ebolavirus glycoprotein that can potentiate the breadth and neutralization potency of other anti-glycoprotein antibodies
Summary for 9BOP
| Entry DOI | 10.2210/pdb9bop/pdb |
| EMDB information | 44747 |
| Descriptor | 11883 heavy chain, 11883 light chain, 11886 heavy chain, ... (8 entities in total) |
| Functional Keywords | ebola, igg, neutralization, complex, glycoprotein, viral protein-immune system complex, ebolavirus, viral protein/immune system |
| Biological source | Oryctolagus cuniculus (rabbit) More |
| Total number of polymer chains | 16 |
| Total formula weight | 298514.89 |
| Authors | Donnellan, F.R.,Rayaprolu, V.,Rijal, P.,O'Dowd, V.,Parvate, A.,Callaway, H.,Hariharan, C.,Parekh, D.,Hui, S.,Shaffer, K.,Hastie, K.,Shimanski, L.,Muller-Krauter, H.,Stecker, T.,Balaram, A.,Halfmann, P.,Saphire, E.O.,Lightwood, D.J.,Townsend, A.R.,Draper, S.J. (deposition date: 2024-05-05, release date: 2025-11-05, Last modification date: 2026-05-20) |
| Primary citation | Donnellan, F.R.,Rayaprolu, V.,Rijal, P.,O'Dowd, V.,Parvate, A.,Callaway, H.,Hariharan, C.,Parekh, D.,Hui, S.,Shaffer, K.C.L.,Avalos, R.D.,Hastie, K.M.,Schimanski, L.,Muller-Krauter, H.,Strecker, T.,Balaram, A.,Halfmann, P.,Saphire, E.O.,Lightwood, D.J.,Townsend, A.R.,Draper, S.J. A broadly-neutralizing antibody against Orthoebolavirus glycoprotein that potentiates the breadth and neutralization of other antibodies. Npj Viruses, 2026 Cited by PubMed Abstract: Ebolavirus disease (EVD) is caused by multiple species of orthoebolavirus. Monoclonal antibodies (mAbs) against the virus glycoprotein (GP) are the only class of therapeutic approved for treatment of EVD caused by Orthoebolavirus zairense (Ebola virus, EBOV). Therefore, mAbs targeting multiple orthoebolavirus species may represent the next generation of EVD therapeutics. Broadly reactive anti-GP mAbs were produced; among these, mAbs 11886 and 11883 were broadly neutralizing in vitro. A 3.0 Å cryo-electron microscopy structure of EBOV GP bound to both mAbs shows that 11886 binds a novel epitope bridging the glycan cap (GC), 3 pocket and GP2 N-terminus, whereas 11883 binds the receptor binding region (RBR) and GC. In vitro, 11886 synergized with a range of mAbs with epitope specificities spanning the RBR/GC, including 11883. Notably, 11886 increased the breadth of neutralization by partner mAbs against different orthoebolavirus species. These data provide a strategic route to design improved mAb-based next-generation EVD therapeutics. PubMed: 42098405DOI: 10.1038/s44298-026-00192-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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