ReviewViruses2012
Structural basis for differential neutralization of ebolaviruses.
Review in Viruses, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
51 citing papers in PubMed, 69 citations in OpenAlex.
- Configurationally Locked Ridaifen-B Analogs as Potent Ebola Virus Entry Inhibitors.Journal of medicinal chemistry · 2026Article
- 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
- Divergent antibody recognition profiles are generated by protective mRNA vaccines against Marburg and Ravn viruses.Nature communications · 2025Article
- Design and characterization of protective pan-ebolavirus and pan-filovirus bispecific antibodies.PLoS pathogens · 2024Article
- Production and Purification of Filovirus Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A Naturally Occurring Polymorphism in the Base of Sudan Virus Glycoprotein Decreases Glycoprotein Stability in a Species-Dependent Manner.Journal of virology · 2021Article
- Prominent Neutralizing Antibody Response Targeting theJournal of virology · 2021Article
- Modulating Neurological Complications of Emerging Infectious Diseases: Mechanistic Approaches to Candidate Phytochemicals.Frontiers in pharmacology · 2021Review
- Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development.Frontiers in immunology · 2021Review
- Global phosphoproteomic analysis of Ebola virions reveals a novel role for VP35 phosphorylation-dependent regulation of genome transcription.Cellular and molecular life sciences : CMLS · 2020Article
- Article
- Polysaccharide Capsules Equip the Human SymbiontJournal of immunology (Baltimore, Md. : 1950) · 2020Article
- Therapeutic monoclonal antibody treatment protects nonhuman primates from severe Venezuelan equine encephalitis virus disease after aerosol exposure.PLoS pathogens · 2019Article
- Antibody responses to viral infections: a structural perspective across three different enveloped viruses.Nature microbiology · 2019Review
- Article
- Structural Basis of Pan-Ebolavirus Neutralization by an Antibody Targeting the Glycoprotein Fusion Loop.Cell reports · 2018Article
- The structural basis for filovirus neutralization by monoclonal antibodies.Current opinion in immunology · 2018Review
- Structural Transition and Antibody Binding of EBOV GP and ZIKV E Proteins from Pre-Fusion to Fusion-Initiation State.Biomolecules · 2018Article
- Design and evaluation of bi- and trispecific antibodies targeting multiple filovirus glycoproteins.The Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
There are five antigenically distinct ebolaviruses that cause hemorrhagic fever in humans or non-human primates (Ebola virus, Sudan virus, Reston virus, Taï Forest virus, and Bundibugyo virus). The small handful of antibodies known to neutralize the ebolaviruses bind to the surface glycoprotein termed GP₁,₂. Curiously, some antibodies against them are known to neutralize in vitro but not protect in vivo, whereas other antibodies are known to protect animal models in vivo, but not neutralize in vitro. A detailed understanding of what constitutes a neutralizing and/or protective antibody response is critical for development of novel therapeutic strategies. Here, we show that paradoxically, a lower affinity antibody with restricted access to its epitope confers better neutralization than a higher affinity antibody against a similar epitope, suggesting that either subtle differences in epitope, or different characteristics of the GP₁,₂ molecules themselves, confer differential neutralization susceptibility. Here, we also report the crystal structure of trimeric, prefusion GP₁,₂ from the original 1976 Boniface variant of Sudan virus complexed with 16F6, the first antibody known to neutralize Sudan virus, and compare the structure to that of Sudan virus, variant Gulu. We discuss new structural details of the GP₁-GP₂ clamp, thermal motion of various regions in GP₁,₂ across the two viruses visualized, details of differential interaction of the crystallized neutralizing antibodies, and their relevance for virus neutralization.
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What OpenQuestion holds
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.