ArticlePLoS neglected tropical diseases2015
Assessment of Inhibitors of Pathogenic Crimean-Congo Hemorrhagic Fever Virus Strains Using Virus-Like Particles.
Article in PLoS neglected tropical diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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.
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Who cites it
47 citing papers in PubMed.
- Pathogenicity and virulence of Crimean-Congo hemorrhagic fever virus: From enzootic maintenance to severe human disease.Virulence · 2026Review
- The Crimean-Congo haemorrhagic fever virus hijacks the liver lipid metabolic pathway for virion production.Emerging microbes & infections · 2026Article
- Structural and functional characterisation of the Crimean-Congo haemorrhagic fever virus RNA dependent RNA polymerase.Nature communications · 2026Article
- Crimean-Congo hemorrhagic fever virus protein GP38 from isolate M18-China confers broad immunological breadth.Research square · 2026Article
- Human antibody targeting Crimean-Congo hemorrhagic fever virus glycoprotein 38 protects mice against heterologous virus challenge.The Journal of clinical investigation · 2026Article
- Article
- Review
- ISG15-USP18 signaling restrains viperin-dependent metabolic antiviral restriction.bioRxiv : the preprint server for biology · 2026Article
- Neutralization of Crimean-Congo hemorrhagic fever pseudotyped virions with heavy chain antibodies.Virologica Sinica · 2025Article
- Article
- Antibodies targeting Crimean-Congo hemorrhagic fever virus GP38 limit vascular leak and viral spread.Science translational medicine · 2025Article
- Engineering and structures of Crimean-Congo hemorrhagic fever virus glycoprotein complexes.Cell · 2025Article
- Murine Models to Study Crimean-Congo Hemorrhagic Fever Hepatic Injury.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Inflammation associated with monocyte/macrophage activation and recruitment corresponds with lethal outcome in a mouse model of Crimean-Congo haemorrhagic feverEmerging microbes & infections · 2024Article
- First Detection of Antibodies Specific to Crimean-Congo Hemorrhagic Fever Virus in Rural Populations of Gabon.The American journal of tropical medicine and hygiene · 2024Article
- Crimean-Congo hemorrhagic fever survivors elicit protective non-neutralizing antibodies that target 11 overlapping regions on glycoprotein GP38.Cell reports · 2024Article
- The low-density lipoprotein receptor and apolipoprotein E associated with CCHFV particles mediate CCHFV entry into cells.Nature communications · 2024Article
- Third International Conference on Crimean-Congo Hemorrhagic Fever in Thessaloniki, Greece, September 19-21, 2023.Antiviral research · 2024Review
- Engineering, structure, and immunogenicity of a Crimean-Congo hemorrhagic fever virus pre-fusion heterotrimeric glycoprotein complex.bioRxiv : the preprint server for biology · 2024Article
- Crimean-Congo Hemorrhagic Fever Survivors Elicit Protective Non-Neutralizing Antibodies that Target 11 Overlapping Regions on Viral Glycoprotein GP38.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Crimean-Congo hemorrhagic fever (CCHF) is an often lethal, acute inflammatory illness that affects a large geographic area. The disease is caused by infection with CCHF virus (CCHFV), a nairovirus from the Bunyaviridae family. Basic research on CCHFV has been severely hampered by biosafety requirements and lack of available strains and molecular tools. We report the development of a CCHF transcription- and entry-competent virus-like particle (tecVLP) system that can be used to study cell entry and viral transcription/replication over a broad dynamic range (~4 orders of magnitude). The tecVLPs are morphologically similar to authentic CCHFV. Incubation of immortalized and primary human cells with tecVLPs results in a strong reporter signal that is sensitive to treatment with neutralizing monoclonal antibodies and by small molecule inhibitors of CCHFV. We used glycoproteins and minigenomes from divergent CCHFV strains to generate tecVLPs, and in doing so, we identified a monoclonal antibody that can prevent cell entry of tecVLPs containing glycoproteins from 3 pathogenic CCHFV strains. In addition, our data suggest that different glycoprotein moieties confer different cellular entry efficiencies, and that glycoproteins from the commonly used strain IbAr10200 have up to 100-fold lower ability to enter primary human cells compared to glycoproteins from pathogenic CCHFV strains.
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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 Socratic graph.