ArticleJournal of virology2011
A new Ebola virus nonstructural glycoprotein expressed through RNA editing.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed, 183 citations in OpenAlex.
- Review
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- Exploring Ebola virus-associated gene expression through comparative analysis.Frontiers in genetics · 2026Article
- Drug Repurposing Investigation for Combating Ebola Virus Disease: Database Mining, Docking Calculations, Molecular Dynamics, and Density Functional Theory Study.ChemistryOpen · 2025Article
- Comparison of the biological properties of bat-derived filovirus envelope glycoproteins.Journal of virology · 2025Article
- Article
- Remdesivir, mAb114, REGN-EB3, and ZMapp partially rescue nonhuman primates infected with a low passage Kikwit variant of Ebola virus.Nature communications · 2025Article
- Quantification of Filovirus Soluble Glycoprotein Using a Sandwich ELISA.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection.PLoS pathogens · 2024Article
- Prospects for the use of viral proteins for the construction of chimeric toxins.Archives of virology · 2024Review
- Afucosylated anti-EBOV antibody MIL77-3 engages sGP to elicit NK cytotoxicity.Journal of virology · 2024Article
- Identification of Prospective Ebola Virus VP35 and VP40 Protein Inhibitors from Myxobacterial Natural Products.Biomolecules · 2024Article
- A compendium of multi-omics data illuminating host responses to lethal human virus infections.Scientific data · 2024Article
- Recent Advances in Therapeutic Approaches Against Ebola Virus Infection.Recent advances in anti-infective drug discovery · 2024Review
- Ebola virus VP35 perturbs type I interferon signaling to facilitate viral replication.Virologica Sinica · 2023Article
- RNA Editing as a General Trait of Ebolaviruses.The Journal of infectious diseases · 2023Article
- Filoviruses: Scientific Gaps and Prototype Pathogen Recommendation.The Journal of infectious diseases · 2023Review
- Antibodies against the Ebola virus soluble glycoprotein are associated with long-term vaccine-mediated protection of non-human primates.Cell reports · 2023Article
- 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
- Pseudotyped Viruses for Marburgvirus and Ebolavirus.Advances in experimental medicine and biology · 2023Article
51 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
Ebola virus (EBOV), an enveloped, single-stranded, negative-sense RNA virus, causes severe hemorrhagic fever in humans and nonhuman primates. The EBOV glycoprotein (GP) gene encodes the nonstructural soluble glycoprotein (sGP) but also produces the transmembrane glycoprotein (GP₁,₂) through transcriptional editing. A third GP gene product, a small soluble glycoprotein (ssGP), has long been postulated to be produced also as a result of transcriptional editing. To identify and characterize the expression of this new EBOV protein, we first analyzed the relative ratio of GP gene-derived transcripts produced during infection in vitro (in Vero E6 cells or Huh7 cells) and in vivo (in mice). The average percentages of transcripts encoding sGP, GP₁,₂, and ssGP were approximately 70, 25, and 5%, respectively, indicating that ssGP transcripts are indeed produced via transcriptional editing. N-terminal sequence similarity with sGP, the absence of distinguishing antibodies, and the abundance of sGP made it difficult to identify ssGP through conventional methodology. Optimized 2-dimensional (2D) gel electrophoresis analyses finally verified the expression and secretion of ssGP in tissue culture during EBOV infection. Biochemical analysis of recombinant ssGP characterized this protein as a disulfide-linked homodimer that was exclusively N glycosylated. In conclusion, we have identified and characterized a new EBOV nonstructural glycoprotein, which is expressed as a result of transcriptional editing of the GP gene. While ssGP appears to share similar structural properties with sGP, it does not appear to have the same anti-inflammatory function on endothelial cells as sGP.
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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.