ArticleNature2008
Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor.
Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 469 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
469 citing papers in PubMed, 731 citations in OpenAlex.
- Computational mining of B cell receptor repertoires reveals antigen-specific and convergent responses to Ebola vaccination.Frontiers in immunology · 2024Trial
- 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
- Pan-Ebolavirus nanoparticle vaccine provides protection in rodents from lethal infection by Zaire and Sudan viruses.Nature communications · 2026Article
- Arming Inactivated Enveloped Virus Vaccines with theVaccines · 2026Review
- Development of Peptide Entry Inhibitors Targeting the Endosomal Receptor NPC1 Binding Site ofPathogens (Basel, Switzerland) · 2026Article
- A broadly-neutralizing antibody against Orthoebolavirus glycoprotein that potentiates the breadth and neutralization of other antibodies.Npj viruses · 2026Article
- Cryo-ET of IgG bivalent binding on SARS-CoV-2 provides structural basis for antibody avidity.Nature communications · 2026Article
- Nanobody targeting glycan cap confers broad orthoebolavirus neutralization.Virologica Sinica · 2026Article
- QSAR-Guided and Fragment-Based Drug Design of Monoterpenoid Inhibitors Targeting Ebola Virus Glycoprotein.International journal of molecular sciences · 2026Article
- A highly potent nanobody-based bispecific therapeutic provides broad-spectrum protection against ebolavirus.Nature communications · 2026Article
- Article
- Computational Design of Broad-Spectrum Ebola Antibodies through Framework and Complementarity-Determining Region Synergistic Optimization.Research (Washington, D.C.) · 2026Article
- Prediction of pre- and postfusion conformations of class I fusion proteins with AlphaFold2.PloS one · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
- A highly potent and broadly accessible bispecific nanobody for the treatment of ebola virus infections.PLoS pathogens · 2026Article
- Structure-Guided Design of Peptide Inhibitors Targeting Class I Viral Fusion Proteins.Pathogens (Basel, Switzerland) · 2025Review
- Rational design of next-generation filovirus vaccines combining glycoprotein stabilization and nanoparticle display with glycan modification.Nature communications · 2025Article
- Biological Breakthroughs and Drug Discovery Revolution via Cryo-Electron Microscopy of Membrane Proteins.Membranes · 2025Review
- A SARS-CoV-2 entry inhibitor trimerizes to lock the spike protein in a closed conformation.bioRxiv : the preprint server for biology · 2025Article
409 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Ebola virus (EBOV) entry requires the surface glycoprotein (GP) to initiate attachment and fusion of viral and host membranes. Here we report the crystal structure of EBOV GP in its trimeric, pre-fusion conformation (GP1+GP2) bound to a neutralizing antibody, KZ52, derived from a human survivor of the 1995 Kikwit outbreak. Three GP1 viral attachment subunits assemble to form a chalice, cradled by the GP2 fusion subunits, while a novel glycan cap and projected mucin-like domain restrict access to the conserved receptor-binding site sequestered in the chalice bowl. The glycocalyx surrounding GP is likely central to immune evasion and may explain why survivors have insignificant neutralizing antibody titres. KZ52 recognizes a protein epitope at the chalice base where it clamps several regions of the pre-fusion GP2 to the amino terminus of GP1. This structure provides a template for unravelling the mechanism of EBOV GP-mediated fusion and for future immunotherapeutic development.
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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.