ArticleVirology journal2005
Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins.
Article in Virology journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
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Who cites it
25 citing papers in PubMed, 59 citations in OpenAlex.
- Tick-host-virus triad in Crimean-Congo hemorrhagic fever transmission: global patterns across vector and reservoir species.Veterinary research communications · 2026Review
- The PACS-2 protein and trafficking motifs in CCHFV Gn and Gc cytoplasmic domains govern CCHFV assembly.Emerging microbes & infections · 2024Article
- Nairovirus polymerase mutations associated with the establishment of persistent infection in human cells.Journal of virology · 2024Article
- Interactome profiling of Crimean-Congo hemorrhagic fever virus glycoproteins.Nature communications · 2023Article
- Segmented, Negative-Sense RNA Viruses of Humans: Genetic Systems and Experimental Uses of Reporter Strains.Annual review of virology · 2023Review
- Article
- Replicating RNA vaccination elicits an unexpected immune response that efficiently protects mice against lethal Crimean-Congo hemorrhagic fever virus challenge.EBioMedicine · 2022Article
- Immunobiology of Crimean-Congo hemorrhagic fever.Antiviral research · 2022Review
- Plant-Derived Recombinant Vaccines against Zoonotic Viruses.Life (Basel, Switzerland) · 2022Review
- Rottlerin inhibits La Crosse virus-induced encephalitis in mice and blocks release of replicating virus from the Golgi body in neurons.Nature microbiology · 2021Article
- The interplays between Crimean-Congo hemorrhagic fever virus (CCHFV) M segment-encoded accessory proteins and structural proteins promote virus assembly and infectivity.PLoS pathogens · 2020Article
- Differential Growth Characteristics of Crimean-Congo Hemorrhagic Fever Virus in Kidney Cells of Human and Bovine Origin.Viruses · 2020Article
- Self-association and subcellular localization of Puumala hantavirus envelope proteins.Scientific reports · 2019Article
- Review
- Review
- A novel vaccine against Crimean-Congo Haemorrhagic Fever protects 100% of animals against lethal challenge in a mouse model.PloS one · 2014Article
- Identification of a putative Crimean-Congo hemorrhagic fever virus entry factor.Biochemical and biophysical research communications · 2011Article
- Inhibition of Hazara nairovirus replication by small interfering RNAs and their combination with ribavirin.Virology journal · 2011Article
- A replication-incompetent Rift Valley fever vaccine: chimeric virus-like particles protect mice and rats against lethal challenge.Virology · 2010Article
- Reverse genetics technology for Rift Valley fever virus: current and future applications for the development of therapeutics and vaccines.Antiviral research · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCrimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment.
resultsFollowing determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins GN and GC, using CMV- and chicken beta-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein GN localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein GC remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of GN.
conclusionThe data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment.
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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.