ArticlemBio2018
Structural Basis of Pan-Ebolavirus Neutralization by a Human Antibody against a Conserved, yet Cryptic Epitope.
Article in mBio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 46 citations in OpenAlex.
- Design of Epitope-Focused Vaccines via Epitope Cleavage.ACS central science · 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
- Marburg Virus Glycoprotein Is a Remarkable Virulent Factor Linked to Hemorrhagic Pathology: Evidence from Multimodal Experimental Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Computational Design of Broad-Spectrum Ebola Antibodies through Framework and Complementarity-Determining Region Synergistic Optimization.Research (Washington, D.C.) · 2026Article
- Discovery of potent cross-neutralizing antibodies against Marburg and Ravn viruses with therapeutic potential.Npj viruses · 2025Article
- Rational design of next-generation filovirus vaccines combining glycoprotein stabilization and nanoparticle display with glycan modification.Nature communications · 2025Article
- Rational design of next-generation filovirus vaccines through glycoprotein stabilization, nanoparticle display, and glycan modification.bioRxiv : the preprint server for biology · 2025Article
- Anti-Ebola virus mAb 3A6 protects highly viremic animals from fatal outcome via binding GPNature communications · 2025Article
- A pan-orthoebolavirus neutralizing antibody encoded by mRNA effectively prevents virus infection.Emerging microbes & infections · 2024Article
- A public, cross-reactive glycoprotein epitope confounds Ebola virus serology.Journal of medical virology · 2024Article
- Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain.Structure (London, England : 1993) · 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
- The evolution and determinants of neutralization of potent head-binding antibodies against Ebola virus.Cell reports · 2023Article
- Structure of the Inmazeb cocktail and resistance to Ebola virus escape.Cell host & microbe · 2023Article
- Glycan shield of the ebolavirus envelope glycoprotein GP.Communications biology · 2022Article
- Review
- Development and Structural Analysis of Antibody Therapeutics for Filoviruses.Pathogens (Basel, Switzerland) · 2022Review
- Article
- Pan-ebolavirus serology study of healthcare workers in the Mbandaka Health Region, Democratic Republic of the Congo.PLoS neglected tropical diseases · 2022Article
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7 authors at 2 institutions in 1 country.
Funding
Abstract
Only one naturally occurring human antibody has been described thus far that is capable of potently neutralizing all five ebolaviruses. Here we present two crystal structures of this rare, pan-ebolavirus neutralizing human antibody in complex with Ebola virus and Bundibugyo virus glycoproteins (GPs), respectively. The structures delineate the key protein and glycan contacts for binding that are conserved across the ebolaviruses, explain the antibody's unique broad specificity and neutralization activity, and reveal the likely mechanism behind a known escape mutation in the fusion loop region of GP2. We found that the epitope of this antibody, ADI-15878, extends along the hydrophobic paddle of the fusion loop and then dips down into a highly conserved pocket beneath the N-terminal tail of GP2, a mode of recognition unlike any other antibody elicited against Ebola virus, and likely critical for its broad activity. The fold of Bundibugyo virus glycoprotein, not previously visualized, is similar to the fold of Ebola virus GP, and ADI-15878 binds to each virus's GP with a similar strategy and angle of attack. These findings will be useful in deployment of this antibody as a broad-spectrum therapeutic and in the design of immunogens that elicit the desired broadly neutralizing immune response against all members of the ebolavirus genus and filovirus family.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.