Observation of arenavirus nucleoprotein heptamer assembly
| Autor: | Papageorgiou, Nicolas, Vaitsopoulou, Afroditi, Diop, Awa, Van Nguyen, Thi, Canard, Bruno, Alvarez, Karine, Ferron, Francois |
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| Přispěvatelé: | Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Aix Marseille Université (AMU), European Virus Bioinformatics Center [Jena], ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-18-ASTR-0010,PaNuVi,Les nucléases virales comme cibles thérapeutiques(2018) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular assembly Bunyavirales Protein Conformation [SDV]Life Sciences [q-bio] viruses RNA-Binding Proteins Arenavirus Recombinant Proteins Viral Proteins Nucleoproteins lcsh:Biology (General) Protein Interaction Domains and Motifs Amino Acid Sequence Protein Multimerization Arenaviridae lcsh:QH301-705.5 Research Articles Research Article nucleoprotein |
| Zdroj: | FEBS Open Bio, Vol 11, Iss 4, Pp 1076-1083 (2021) FEBS Open Bio FEBS Open Bio, 2021, ⟨10.1002/2211-5463.13106⟩ FEBS Open Bio, Wiley Open Access/Elsevier, 2021, ⟨10.1002/2211-5463.13106⟩ |
| ISSN: | 2211-5463 |
| DOI: | 10.1002/2211-5463.13106⟩ |
| Popis: | Arenaviruses are enveloped viruses containing a segmented, negative, and ambisense single‐stranded RNA genome wrapped with a nucleoprotein (NP). The NP is the most abundant viral protein in infected cells and plays a critical role in both replication/transcription and virion assembly. The NP associates with RNA to form a ribonucleoprotein (RNP) complex, and this implies self‐assembly while the exact structure of this polymer is not yet known. Here, we report a measurement of the full‐length Mopeia virus NP by negative stain transmission electron microscopy. We observed RNP complex particles with diameter 15 ± 1 nm as well as symmetric circular heptamers of the same diameter, consistent with previous observations. The nucleoprotein associates with RNA to form a ribonucleoprotein complex. The nucleoprotein trends to self‐assemble into heptameric rings. Theses rings represent stable intermediate states representative of the average full turn of the Arenaviridae ribonucleoprotein filament. They are the first observation of the complexed nucleoprotein‐RNA as a polymer and hint that oligomerization occurs as it happens for other Bunyavirales nucleoproteins. |
| Databáze: | OpenAIRE |
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