ArticlePloS one2014
High-resolution structure of the N-terminal endonuclease domain of the Lassa virus L polymerase in complex with magnesium ions.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 37 citations in OpenAlex.
- Perspectives for pharmaceutical screening at XFEL sources using the example of Lassa virus endonuclease.Acta crystallographica. Section D, Structural biology · 2026Article
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- Structural snapshots of phenuivirus cap-snatching and transcription.Nucleic acids research · 2024Article
- 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
- Insights into Two-Metal-Ion Catalytic Mechanism of Cap-Snatching Endonuclease of Ebinur Lake Virus inJournal of virology · 2022Article
- Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity.Nature communications · 2021Article
- Pathogenicity and virulence mechanisms of Lassa virus and its animal modeling, diagnostic, prophylactic, and therapeutic developments.Virulence · 2021Review
- Article
- Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation.Nature microbiology · 2020Article
- Biochemical characterization of the Lassa virus L protein.The Journal of biological chemistry · 2019Article
- Structure of a functional cap-binding domain in Rift Valley fever virus L protein.PLoS pathogens · 2019Article
- Biochemical and structural studies reveal differences and commonalities among cap-snatching endonucleases from segmented negative-strand RNA viruses.The Journal of biological chemistry · 2018Article
- Crystal structures ofIUCrJ · 2018Article
- Rice Stripe Tenuivirus Has a Greater Tendency To Use the Prime-and-Realign Mechanism in Transcription of Genomic than in Transcription of Antigenomic Template RNAs.Journal of virology · 2018Article
- Structural insights into reptarenavirus cap-snatching machinery.PLoS pathogens · 2017Article
- Transcription and replication mechanisms of Bunyaviridae and Arenaviridae L proteins.Virus research · 2017Review
- Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion Morphogenesis.Journal of virology · 2016Article
- Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases.PLoS pathogens · 2016Article
- Atomic Structure and Biochemical Characterization of an RNA Endonuclease in the N Terminus of Andes Virus L Protein.PLoS pathogens · 2016Article
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7 authors at 3 institutions in 3 countries.
Funding
Abstract
Lassa virus (LASV) causes deadly hemorrhagic fever disease for which there are no vaccines and limited treatments. LASV-encoded L polymerase is required for viral RNA replication and transcription. The functional domains of L-a large protein of 2218 amino acid residues-are largely undefined, except for the centrally located RNA-dependent RNA polymerase (RdRP) motif. Recent structural and functional analyses of the N-terminal region of the L protein from lymphocytic choriomeningitis virus (LCMV), which is in the same Arenaviridae family as LASV, have identified an endonuclease domain that presumably cleaves the cap structures of host mRNAs in order to initiate viral transcription. Here we present a high-resolution crystal structure of the N-terminal 173-aa region of the LASV L protein (LASV L173) in complex with magnesium ions at 1.72 Å. The structure is highly homologous to other known viral endonucleases of arena- (LCMV NL1), orthomyxo- (influenza virus PA), and bunyaviruses (La Crosse virus NL1). Although the catalytic residues (D89, E102 and K122) are highly conserved among the known viral endonucleases, LASV L endonuclease structure shows some notable differences. Our data collected from in vitro endonuclease assays and a reporter-based LASV minigenome transcriptional assay in mammalian cells confirm structural prediction of LASV L173 as an active endonuclease. The high-resolution structure of the LASV L endonuclease domain in complex with magnesium ions should aid the development of antivirals against lethal Lassa hemorrhagic fever.
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