ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of the Leanyer orthobunyavirus nucleoprotein-RNA complex reveals unique architecture for RNA encapsidation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 62 citations in OpenAlex.
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- Isolation of Reconstructed Functional Ribonucleoprotein Complexes of Machupo Virus.Journal of virology · 2021Article
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- Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus.Journal of virology · 2020Article
- Structural and functional similarities in bunyaviruses: Perspectives for pan-bunya antivirals.Reviews in medical virology · 2019Review
- Identification and localization of Tospovirus genus-wide conserved residues in 3D models of the nucleocapsid and the silencing suppressor proteins.Virology journal · 2019Article
- Complementary Mutations in the N and L Proteins for Restoration of Viral RNA Synthesis.Journal of virology · 2018Article
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- Distinct Mechanism for the Formation of the Ribonucleoprotein Complex of Tomato Spotted Wilt Virus.Journal of virology · 2017Article
- Asymmetric Trimeric Ring Structure of the Nucleocapsid Protein of Tospovirus.Journal of virology · 2017Article
- Homology modeling and molecular dynamics provide structural insights into tospovirus nucleoprotein.BMC bioinformatics · 2016Article
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11 authors at 6 institutions in 2 countries.
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Abstract
Negative-stranded RNA viruses cover their genome with nucleoprotein (N) to protect it from the human innate immune system. Abrogation of the function of N offers a unique opportunity to combat the spread of the viruses. Here, we describe a unique fold of N from Leanyer virus (LEAV, Orthobunyavirus genus, Bunyaviridae family) in complex with single-stranded RNA refined to 2.78 Å resolution as well as a 2.68 Å resolution structure of LEAV N-ssDNA complex. LEAV N is made up of an N- and a C-terminal lobe, with the RNA binding site located at the junction of these lobes. The LEAV N tetramer binds a 44-nucleotide-long single-stranded RNA chain. Hence, oligomerization of N is essential for encapsidation of the entire genome and is accomplished by using extensions at the N and C terminus. Molecular details of the oligomerization of N are illustrated in the structure where a circular ring-like tertiary assembly of a tetramer of LEAV N is observed tethering the RNA in a positively charged cavity running along the inner edge. Hydrogen bonds between N and the C2 hydroxyl group of ribose sugar explain the specificity of LEAV N for RNA over DNA. In addition, base-specific hydrogen bonds suggest that some regions of RNA bind N more tightly than others. Hinge movements around F20 and V125 assist in the reversal of capsidation during transcription and replication of the virus. Electron microscopic images of the ribonucleoprotein complexes of LEAV N reveal a filamentous assembly similar to those found in phleboviruses.
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