ArticleNature communications2018
Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed.
- Differential glycosylation in the envelope glycoprotein enhances DC-SIGN-mediated cell entry of the West African Ebolavirus Makona.Emerging microbes & infections · 2026Article
- A small molecule inhibits Ebola virus entry through glycoprotein stabilization.Nature communications · 2026Article
- Benchmarking AlphaFold and related deep learning approaches for modeling antibody and TCR antigen recognition.bioRxiv : the preprint server for biology · 2026Article
- Achievements and Challenges in Therapy and Vaccines Development of Viral Hemorrhagic Fevers: An Up-to-Date Review.Pharmaceutics · 2026Review
- 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
- Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection.PLoS pathogens · 2024Article
- Delayed treatment of cynomolgus macaques with a FVM04/CA45 monoclonal antibody cocktail provides complete protection against lethal Sudan virus infection.Journal of virology · 2024Article
- Macaque antibodies targeting Marburg virus glycoprotein induced by multivalent immunization.Journal of virology · 2024Article
- The evolution and determinants of neutralization of potent head-binding antibodies against Ebola virus.Cell reports · 2023Article
- Regions of hepatitis C virus E2 required for membrane association.Nature communications · 2023Article
- Skin Vaccination with Ebola Virus Glycoprotein Using a Polyphosphazene-Based Microneedle Patch Protects Mice against Lethal Challenge.Journal of functional biomaterials · 2022Article
- Development and Structural Analysis of Antibody Therapeutics for Filoviruses.Pathogens (Basel, Switzerland) · 2022Review
- Filovirus Neutralising Antibodies: Mechanisms of Action and Therapeutic Application.Pathogens (Basel, Switzerland) · 2021Review
- Using the antibody-antigen binding interface to train image-based deep neural networks for antibody-epitope classification.PLoS computational biology · 2021Article
- Article
- Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development.Frontiers in immunology · 2021Review
- Article
- Designs and Characterization of Subunit Ebola GP Vaccine Candidates: Implications for Immunogenicity.Frontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The severity of the 2014-2016 ebolavirus outbreak in West Africa expedited clinical development of therapeutics and vaccines though the countermeasures on hand were largely monospecific and lacked efficacy against other ebolavirus species that previously emerged. Recent studies indicate that ebolavirus glycoprotein (GP) fusion loops are targets for cross-protective antibodies. Here we report the 3.72 Å resolution crystal structure of one such cross-protective antibody, CA45, bound to the ectodomain of Ebola virus (EBOV) GP. The CA45 epitope spans multiple faces of the fusion loop stem, across both GP1 and GP2 subunits, with ~68% of residues identical across > 99.5% of known ebolavirus isolates. Extensive antibody interactions within a pan-ebolavirus small-molecule inhibitor binding cavity on GP define this cavity as a novel site of immune vulnerability. The structure elucidates broad ebolavirus neutralization through a highly conserved epitope on GP and further enables rational design and development of broadly protective vaccines and therapeutics.
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