ArticleJournal of virology2012
Structure of Crimean-Congo hemorrhagic fever virus nucleoprotein: superhelical homo-oligomers and the role of caspase-3 cleavage.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 87 citations in OpenAlex.
- Structural and mechanistic insights into protective non-neutralizing antibodies targeting Crimean-Congo hemorrhagic fever virus nucleocapsid protein.Nature communications · 2026Article
- Solution Structure of Nucleoprotein Domain 1 from the Emerging Yezo Virus.International journal of molecular sciences · 2026Article
- Review
- Integrated surveillance, virus isolation and phylogenetic characterization of Crimean-Congo hemorrhagic fever virus in Central Kazakhstan.Frontiers in veterinary science · 2026Article
- Review
- Crimean-Congo Hemorrhagic Fever Virus Infections in Slaughtered Camels and Abattoir Workers in the United Arab Emirates.Transboundary and emerging diseases · 2025Article
- Article
- Identification of critical residues for RNA binding of nairovirus nucleoprotein.Journal of virology · 2024Article
- The Role of Nucleocapsid Protein (NP) in the Immunology of Crimean-Congo Hemorrhagic Fever Virus (CCHFV).Viruses · 2024Review
- Crimean Congo Hemorrhagic Fever Virus for Clinicians-Virology, Pathogenesis, and Pathology.Emerging infectious diseases · 2024Review
- Nairovirus polymerase mutations associated with the establishment of persistent infection in human cells.Journal of virology · 2024Article
- Alternative translation contributes to the generation of a cytoplasmic subpopulation of the Junín virus nucleoprotein that inhibits caspase activation and innate immunity.Journal of virology · 2024Article
- The Phlebovirus Ribonucleoprotein: An Overview.Methods in molecular biology (Clifton, N.J.) · 2024Review
- The mechanism of genome replication and transcription in bunyaviruses.PLoS pathogens · 2023Review
- Immunobiology of Crimean-Congo hemorrhagic fever.Antiviral research · 2022Review
- Genomic characterization and phylogenetic analysis of a novel Nairobi sheep disease genogroup Orthonairovirus from ticks, Southeastern China.Frontiers in microbiology · 2022Article
- Immune responses in multiple hosts to Nucleocapsid Protein (NP) of Crimean-Congo Hemorrhagic Fever Virus (CCHFV).PLoS neglected tropical diseases · 2021Article
- Presence of antibodies to Crimean Congo haemorrhagic fever virus in sheep in Tunisia, North Africa.Veterinary medicine and science · 2021Article
- Crimean-Congo Hemorrhagic Fever Virus: Current Advances and Future Prospects of Antiviral Strategies.Viruses · 2021Review
- Purification of Crimean-Congo hemorrhagic fever virus nucleoprotein and its utility for serological diagnosis.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crimean-Congo hemorrhagic fever, a severe hemorrhagic disease found throughout Africa, Europe, and Asia, is caused by the tick-borne Crimean-Congo hemorrhagic fever virus (CCHFV). CCHFV is a negative-sense single-stranded RNA (ssRNA) virus belonging to the Nairovirus genus of the Bunyaviridae family. Its genome of three single-stranded RNA segments is encapsidated by the nucleocapsid protein (CCHFV N) to form the ribonucleoprotein complex. This ribonucleoprotein complex is required during replication and transcription of the viral genomic RNA. Here, we present the crystal structures of the CCHFV N in two distinct forms, an oligomeric form comprised of double antiparallel superhelices and a monomeric form. The head-to-tail interaction of the stalk region of one CCHFV N subunit with the base of the globular body of the adjacent subunit stabilizes the helical organization of the oligomeric form of CCHFV N. It also masks the conserved caspase-3 cleavage site present at the tip of the stalk region from host cell caspase-3 interaction and cleavage. By incubation with primer-length ssRNAs, we also obtained the crystal structure of CCHFV N in its monomeric form, which is similar to a recently published structure. The conformational change of CCHFV N upon deoligomerization results in the exposure of the caspase-3 cleavage site and subjects CCHFV N to caspase-3 cleavage. Mutations of this cleavage site inhibit cleavage by caspase-3 and result in enhanced viral polymerase activity. Thus, cleavage of CCHFV N by host cell caspase-3 appears to be crucial for controlling viral RNA synthesis and represents an important host defense mechanism against CCHFV infection.
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