ArticleNature communications2019
Cross-reactive neutralizing human survivor monoclonal antibody BDBV223 targets the ebolavirus stalk.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Pan-Ebolavirus nanoparticle vaccine provides protection in rodents from lethal infection by Zaire and Sudan viruses.Nature communications · 2026Article
- Bundibugyo Virus Disease: Diagnostics and Medical Countermeasures for a Neglected Ebolavirus.Viruses · 2026Review
- Mapping the global evidence base of bundibugyo ebolavirus disease: a systematic scoping review of research gaps and preparedness priorities.BMC infectious diseases · 2026Article
- Anti-Ebola virus mAb 3A6 protects highly viremic animals from fatal outcome via binding GPNature communications · 2025Article
- Review
- Antibodies targeting the glycan cap of Ebola virus glycoprotein are potent inducers of the complement systemCommunications biology · 2024Article
- Anti-Ebola virus mAb 3A6 with unprecedented potency protects highly viremic animals from fatal outcome and physically lifts its glycoprotein target from the virion membrane.Research square · 2023Article
- Inadequate structural constraint on Fab approach rather than paratope elicitation limits HIV-1 MPER vaccine utility.Nature communications · 2023Article
- Review
- Epitope-focused immunogen design based on the ebolavirus glycoprotein HR2-MPER region.PLoS pathogens · 2022Article
- Development and Structural Analysis of Antibody Therapeutics for Filoviruses.Pathogens (Basel, Switzerland) · 2022Review
- A Naturally Occurring Polymorphism in the Base of Sudan Virus Glycoprotein Decreases Glycoprotein Stability in a Species-Dependent Manner.Journal of virology · 2021Article
- Ebola vaccine-induced protection in nonhuman primates correlates with antibody specificity and Fc-mediated effects.Science translational medicine · 2021Article
- Structural basis for broad coronavirus neutralization.Nature structural & molecular biology · 2021Article
- Single-component multilayered self-assembling nanoparticles presenting rationally designed glycoprotein trimers as Ebola virus vaccines.Nature communications · 2021Article
- Convergence of a common solution for broad ebolavirus neutralization by glycan cap-directed human antibodies.Cell reports · 2021Article
- A conserved immunogenic and vulnerable site on the coronavirus spike protein delineated by cross-reactive monoclonal antibodies.Nature communications · 2021Article
- Evidence for distinct mechanisms of small molecule inhibitors of filovirus entry.PLoS pathogens · 2021Article
- Structural basis for broad coronavirus neutralization.bioRxiv : the preprint server for biology · 2021Article
- Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development.Frontiers in immunology · 2021Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Three Ebolavirus genus viruses cause lethal disease and lack targeted therapeutics: Ebola virus, Sudan virus and Bundibugyo virus. Monoclonal antibody (mAb) cocktails against the surface glycoprotein (GP) present a potential therapeutic strategy. Here we report two crystal structures of the antibody BDBV223, alone and complexed with its GP2 stalk epitope, an interesting site for therapeutic/vaccine design due to its high sequence conservation among ebolaviruses. BDBV223, identified in a human survivor of Bundibugyo virus disease, neutralizes both Bundibugyo virus and Ebola virus, but not Sudan virus. Importantly, the structure suggests that BDBV223 binding interferes with both the trimeric bundle assembly of GP and the viral membrane by stabilizing a conformation in which the monomers are separated by GP lifting or bending. Targeted mutagenesis of BDBV223 to enhance SUDV GP recognition indicates that additional determinants of antibody binding likely lie outside the visualized interactions, and perhaps involve quaternary assembly or membrane-interacting regions.
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