6QD7
EM structure of a EBOV-GP bound to 3T0331 neutralizing antibody
Summary for 6QD7
| Entry DOI | 10.2210/pdb6qd7/pdb |
| EMDB information | 4520 |
| Descriptor | Light chain, Heavy chain, Envelope glycoprotein,Virion spike glycoprotein,EBOV-GP1, ... (7 entities in total) |
| Functional Keywords | antibody, immune response, viral infection, ebov, viral protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 12 |
| Total formula weight | 306034.36 |
| Authors | Diskin, R.,Cohen-Dvashi, H. (deposition date: 2019-01-01, release date: 2019-10-02, Last modification date: 2024-10-16) |
| Primary citation | Ehrhardt, S.A.,Zehner, M.,Krahling, V.,Cohen-Dvashi, H.,Kreer, C.,Elad, N.,Gruell, H.,Ercanoglu, M.S.,Schommers, P.,Gieselmann, L.,Eggeling, R.,Dahlke, C.,Wolf, T.,Pfeifer, N.,Addo, M.M.,Diskin, R.,Becker, S.,Klein, F. Polyclonal and convergent antibody response to Ebola virus vaccine rVSV-ZEBOV. Nat. Med., 25:1589-1600, 2019 Cited by PubMed Abstract: Recombinant vesicular stomatitis virus-Zaire Ebola virus (rVSV-ZEBOV) is the most advanced Ebola virus vaccine candidate and is currently being used to combat the outbreak of Ebola virus disease (EVD) in the Democratic Republic of the Congo (DRC). Here we examine the humoral immune response in a subset of human volunteers enrolled in a phase 1 rVSV-ZEBOV vaccination trial by performing comprehensive single B cell and electron microscopy structure analyses. Four studied vaccinees show polyclonal, yet reproducible and convergent B cell responses with shared sequence characteristics. EBOV-targeting antibodies cross-react with other Ebolavirus species, and detailed epitope mapping revealed overlapping target epitopes with antibodies isolated from EVD survivors. Moreover, in all vaccinees, we detected highly potent EBOV-neutralizing antibodies with activities comparable or superior to the monoclonal antibodies currently used in clinical trials. These include antibodies combining the IGHV3-15/IGLV1-40 immunoglobulin gene segments that were identified in all investigated individuals. Our findings will help to evaluate and direct current and future vaccination strategies and offer opportunities for novel EVD therapies. PubMed: 31591605DOI: 10.1038/s41591-019-0602-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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