ArticleImmunity2018
Multifunctional Pan-ebolavirus Antibody Recognizes a Site of Broad Vulnerability on the Ebolavirus Glycoprotein.
Article in Immunity, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
53 citing papers in PubMed, 84 citations in OpenAlex.
- Computational mining of B cell receptor repertoires reveals antigen-specific and convergent responses to Ebola vaccination.Frontiers in immunology · 2024Trial
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- The 2026 Bundibugyo virus disease outbreak in the Democratic Republic of the Congo: Virology, epidemiology, continental response, and research priorities.Infectious medicine · 2026Review
- 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
- A broadly-neutralizing antibody against Orthoebolavirus glycoprotein that potentiates the breadth and neutralization of other antibodies.Npj viruses · 2026Article
- A highly potent nanobody-based bispecific therapeutic provides broad-spectrum protection against ebolavirus.Nature communications · 2026Article
- Article
- Rational design of next-generation filovirus vaccines combining glycoprotein stabilization and nanoparticle display with glycan modification.Nature communications · 2025Article
- HIV broadly neutralizing antibody precursors to the Apex epitope induced in nonhuman primates.Science immunology · 2025Article
- Rational design of next-generation filovirus vaccines through glycoprotein stabilization, nanoparticle display, and glycan modification.bioRxiv : the preprint server for biology · 2025Article
- A pan-orthoebolavirus neutralizing antibody encoded by mRNA effectively prevents virus infection.Emerging microbes & infections · 2024Article
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- Antibodies targeting the glycan cap of Ebola virus glycoprotein are potent inducers of the complement systemCommunications biology · 2024Article
- A Pan-Ebolavirus Monoclonal Antibody Cocktail Provides Protection Against Ebola and Sudan Viruses.The Journal of infectious diseases · 2023Article
- Blocking of ebolavirus spread through intercellular connections by an MPER-specific antibody depends on BST2/tetherin.Cell reports · 2023Article
- Structural and mechanistic basis of neutralization by a pan-hantavirus protective antibody.Science translational medicine · 2023Article
- Systematic analysis of human antibody response to ebolavirus glycoprotein shows high prevalence of neutralizing public clonotypes.Cell reports · 2023Article
- Monoclonal antibody therapeutics for infectious diseases: Beyond normal human immunoglobulin.Pharmacology & therapeutics · 2022Review
- Epitope-focused immunogen design based on the ebolavirus glycoprotein HR2-MPER region.PLoS pathogens · 2022Article
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Authors and funding
32 authors at 11 institutions in 2 countries.
Funding
Abstract
Ebolaviruses cause severe disease in humans, and identification of monoclonal antibodies (mAbs) that are effective against multiple ebolaviruses are important for therapeutics development. Here we describe a distinct class of broadly neutralizing human mAbs with protective capacity against three ebolaviruses infectious for humans: Ebola (EBOV), Sudan (SUDV), and Bundibugyo (BDBV) viruses. We isolated mAbs from human survivors of ebolavirus disease and identified a potent mAb, EBOV-520, which bound to an epitope in the glycoprotein (GP) base region. EBOV-520 efficiently neutralized EBOV, BDBV, and SUDV and also showed protective capacity in relevant animal models of these infections. EBOV-520 mediated protection principally by direct virus neutralization and exhibited multifunctional properties. This study identified a potent naturally occurring mAb and defined key features of the human antibody response that may contribute to broad protection. This multifunctional mAb and related clones are promising candidates for development as broadly protective pan-ebolavirus therapeutic molecules.
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Registered trials
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.