ArticlePLoS pathogens2019
Structure of a functional cap-binding domain in Rift Valley fever virus L protein.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Genetic Adaptation Accompanying the Emergence of Inkoo Virus, the European Orthobunyavirus jamestownense.Annals of the New York Academy of Sciences · 2026Article
- Opportunities and challenges for countermeasures against Rift Valley fever virus: A quintessential One Health pathogen.PLoS neglected tropical diseases · 2026Review
- Structures of the Crimean-Congo hemorrhagic fever virus RNA-dependent RNA polymerase.Cell discovery · 2026Article
- Microbial pigments as potential anti-rift valley fever virus drugs.BMC chemistry · 2026Article
- Review
- Article
- Structural snapshots of phenuivirus cap-snatching and transcription.Nucleic acids research · 2024Article
- Limited high-throughput screening compatibility of the phenuivirus cap-binding domain.Scientific reports · 2023Article
- Structural and functional characterization of the Sin Nombre virus L protein.PLoS pathogens · 2023Article
- Genetic variants of Dabie bandavirus: classification and biological/clinical implications.Virology journal · 2023Review
- Identifying the genetic basis of viral spillover using Lassa virus as a test case.Royal Society open science · 2023Article
- Structural insights into viral genome replication by the severe fever with thrombocytopenia syndrome virus L protein.Nucleic acids research · 2023Article
- Host entry factors of Rift Valley Fever Virus infection.Advances in virus research · 2023Article
- The mechanism of genome replication and transcription in bunyaviruses.PLoS pathogens · 2023Review
- Article
- Structural Elucidation of Rift Valley Fever Virus L Protein towards the Discovery of Its Potential Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Structure of Rift Valley Fever Virus RNA-Dependent RNA Polymerase.Journal of virology · 2022Article
- Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity.Nature communications · 2021Article
- Distribution and Molecular Identification ofPathogens (Basel, Switzerland) · 2021Article
- Computing the Structural Dynamics of RVFV L Protein Domain in Aqueous Glycerol Solutions.Biomolecules · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rift Valley fever virus (RVFV) belongs to the family of Phenuiviridae within the order of Bunyavirales. The virus may cause fatal disease both in livestock and humans, and therefore, is of great economical and public health relevance. In analogy to the influenza virus polymerase complex, the bunyavirus L protein is assumed to bind to and cleave off cap structures of cellular mRNAs to prime viral transcription. However, even though the presence of an endonuclease in the N-terminal domain of the L protein has been demonstrated for several bunyaviruses, there is no evidence for a cap-binding site within the L protein. We solved the structure of a C-terminal 117 amino acid-long domain of the RVFV L protein by X-ray crystallography. The overall fold of the domain shows high similarity to influenza virus PB2 cap-binding domain and the putative non-functional cap-binding domain of reptarenaviruses. Upon co-crystallization with m7GTP, we detected the cap-analogue bound between two aromatic side chains as it has been described for other cap-binding proteins. We observed weak but specific interaction with m7GTP rather than GTP in vitro using isothermal titration calorimetry. The importance of m7GTP-binding residues for viral transcription was validated using a RVFV minigenome system. In summary, we provide structural and functional evidence for a cap-binding site located within the L protein of a virus from the Bunyavirales order.
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