ArticleNature microbiology2016
Structures of Ebola virus GP and sGP in complex with therapeutic antibodies.
Article in Nature microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
What it found
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Who cites it
81 citing papers in PubMed.
- Review
- Confirming ERVEBO Vaccination to Support Ebola Virus Surveillance.Emerging infectious diseases · 2026Article
- Nanobody targeting glycan cap confers broad orthoebolavirus neutralization.Virologica Sinica · 2026Article
- Oriented Multivalent Display Drives Consistent Serum Immunodominance to the Ebola Virus Glycoprotein.ACS central science · 2026Article
- A highly potent and broadly accessible bispecific nanobody for the treatment of ebola virus infections.PLoS pathogens · 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
- Surface Plasmon Resonance for the Interaction of Capsular Polysaccharide (CPS) With KpACE.Bio-protocol · 2025Article
- Mapping Immunological, Host Receptor Binding Determinants, and Cathepsin Cleavage Site of EBOV Glycoprotein Utilizing the Qubevirus Platform.ACS omega · 2025Article
- Treatment of Ebola Virus Disease: From Serotherapy to the Use of Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2025Review
- Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection.PLoS pathogens · 2024Article
- Review
- Multivalent Protein-Nucleic Acid Interactions Probed by Composition-Gradient Multiangle Light Scattering.ACS omega · 2024Article
- A lethal mice model of recombinant vesicular stomatitis viruses for EBOV-targeting prophylactic vaccines evaluation.Virologica Sinica · 2024Article
- Growing Glycans in Rosetta: Accurate de novo glycan modeling, density fitting, and rational sequon design.PLoS computational biology · 2024Article
- Review
- Structurally Different Yet Functionally Similar: Aptamers Specific for the Ebola Virus Soluble Glycoprotein and GP1,2 and Their Application in Electrochemical Sensing.International journal of molecular sciences · 2023Article
- Ebola virus protein VP40 stimulates IL-12- and IL-18-dependent activation of human natural killer cells.JCI insight · 2022Article
- Recent Progress in the Discovery and Development of Monoclonal Antibodies against Viral Infections.Biomedicines · 2022Review
- Rapid detection of an Ebola biomarker with optical microring resonators.Cell reports methods · 2022Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
The Ebola virus (EBOV) GP gene encodes two glycoproteins. The major product is a soluble, dimeric glycoprotein (sGP) that is secreted abundantly. Despite the abundance of sGP during infection, little is known regarding its structure or functional role. A minor product, resulting from transcriptional editing, is the transmembrane-anchored, trimeric viral surface glycoprotein (GP). GP mediates attachment to and entry into host cells, and is the intended target of antibody therapeutics. Because large portions of sequence are shared between GP and sGP, it has been hypothesized that sGP may potentially subvert the immune response or may contribute to pathogenicity. In this study, we present cryo-electron microscopy structures of GP and sGP in complex with GP-specific and GP/sGP cross-reactive antibodies undergoing human clinical trials. The structure of the sGP dimer presented here, in complex with both an sGP-specific antibody and a GP/sGP cross-reactive antibody, permits us to unambiguously assign the oligomeric arrangement of sGP and compare its structure and epitope presentation to those of GP. We also provide biophysical evaluation of naturally occurring GP/sGP mutations that fall within the footprints identified by our high-resolution structures. Taken together, our data provide a detailed and more complete picture of the accessible Ebolavirus glycoprotein landscape and a structural basis to evaluate patient and vaccine antibody responses towards differently structured products of the GP gene.
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