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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 DOI10.2210/pdb9bop/pdb
EMDB information44747
Descriptor11883 heavy chain, 11883 light chain, 11886 heavy chain, ... (8 entities in total)
Functional Keywordsebola, igg, neutralization, complex, glycoprotein, viral protein-immune system complex, ebolavirus, viral protein/immune system
Biological sourceOryctolagus cuniculus (rabbit)
More
Total number of polymer chains16
Total formula weight298514.89
Authors
Primary citationDonnellan, 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: 42098405
DOI: 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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PDB entries from 2026-05-20

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