ArticleThe Journal of biological chemistry2018
Biochemical and structural studies reveal differences and commonalities among cap-snatching endonucleases from segmented negative-strand RNA viruses.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 45 citations in OpenAlex.
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- Structural and functional characterisation of the Crimean-Congo haemorrhagic fever virus RNA dependent RNA polymerase.Nature communications · 2026Article
- Structure and function of the nairovirus cap-snatching endonuclease.Nucleic acids research · 2026Article
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- Salvianolic acid A from Salvia miltiorrhiza identified as a cap-dependent endonuclease inhibitor for pathogenic arenaviruses.Acta pharmacologica Sinica · 2026Article
- Identification and Characterization of a Metal Binding-Independent Rift Valley Fever Virus Endonuclease Inhibitor.ACS infectious diseases · 2025Article
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- ICTV Virus Taxonomy Profile:The Journal of general virology · 2024Article
- Crimean-Congo haemorrhagic fever virus.Nature reviews. Microbiology · 2023Review
- Structural insights into viral genome replication by the severe fever with thrombocytopenia syndrome virus L protein.Nucleic acids research · 2023Article
- The mechanism of genome replication and transcription in bunyaviruses.PLoS pathogens · 2023Review
- Identification of cap-dependent endonuclease inhibitors with broad-spectrum activity against bunyaviruses.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Virtual screening of phytochemicals from Indian medicinal plants against the endonuclease domain of SFTS virus L polymerase.RSC advances · 2022Article
- Structure of Rift Valley Fever Virus RNA-Dependent RNA Polymerase.Journal of virology · 2022Article
- Mass Spectrometry-Based Structural Proteomics for Metal Ion/Protein Binding Studies.Biomolecules · 2022Review
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- Isolation of Reconstructed Functional Ribonucleoprotein Complexes of Machupo Virus.Journal of virology · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viruses rely on many host cell processes, including the cellular transcription machinery. Segmented negative-strand RNA viruses (sNSV) in particular cannot synthesize the 5'-cap structure for their mRNA but cleave off cellular caps and use the resulting oligonucleotides as primers for their transcription. This cap-snatching mechanism, involving a viral cap-binding site and RNA endonuclease, is both virus-specific and essential for viral proliferation and therefore represents an attractive drug target. Here, we present biochemical and structural results on the putative cap-snatching endonuclease of Crimean-Congo hemorrhagic fever virus (CCHFV), a highly pathogenic bunyavirus belonging to the Nairoviridae family, and of two additional nairoviruses, Erve virus (EREV) and Nairobi sheep disease virus (NSDV). Our findings are presented in the context of other cap-snatching endonucleases, such as the enzymatically active endonuclease from Rift Valley fever virus (RVFV), from Arenaviridae and Bunyavirales, belonging to the His- and His+ endonucleases, respectively, according to the absence or presence of a metal ion-coordinating histidine in the active site. Mutational and metal-binding experiments revealed the presence of only acidic metal-coordinating residues in the active site of the CCHFV domain and a unique active-site conformation that was intermediate between those of His+ and His- endonucleases. On the basis of small-angle X-ray scattering (SAXS) and homology modeling results, we propose a protein topology for the CCHFV domain that, despite its larger size, has a structure overall similar to those of related endonucleases. These results suggest structural and functional conservation of the cap-snatching mechanism among sNSVs.
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