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Observation of arenavirus nucleoprotein heptamer assembly
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 associa...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8016135/ https://www.ncbi.nlm.nih.gov/pubmed/33534950 http://dx.doi.org/10.1002/2211-5463.13106 |
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author | Papageorgiou, Nicolas Vaitsopoulou, Afroditi Diop, Awa Nguyen, Thi Hong Van Canard, Bruno Alvarez, Karine Ferron, François |
author_facet | Papageorgiou, Nicolas Vaitsopoulou, Afroditi Diop, Awa Nguyen, Thi Hong Van Canard, Bruno Alvarez, Karine Ferron, François |
author_sort | Papageorgiou, Nicolas |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8016135 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-80161352021-04-02 Observation of arenavirus nucleoprotein heptamer assembly Papageorgiou, Nicolas Vaitsopoulou, Afroditi Diop, Awa Nguyen, Thi Hong Van Canard, Bruno Alvarez, Karine Ferron, François FEBS Open Bio Research Articles 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. John Wiley and Sons Inc. 2021-02-25 /pmc/articles/PMC8016135/ /pubmed/33534950 http://dx.doi.org/10.1002/2211-5463.13106 Text en © 2021 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Papageorgiou, Nicolas Vaitsopoulou, Afroditi Diop, Awa Nguyen, Thi Hong Van Canard, Bruno Alvarez, Karine Ferron, François Observation of arenavirus nucleoprotein heptamer assembly |
title | Observation of arenavirus nucleoprotein heptamer assembly |
title_full | Observation of arenavirus nucleoprotein heptamer assembly |
title_fullStr | Observation of arenavirus nucleoprotein heptamer assembly |
title_full_unstemmed | Observation of arenavirus nucleoprotein heptamer assembly |
title_short | Observation of arenavirus nucleoprotein heptamer assembly |
title_sort | observation of arenavirus nucleoprotein heptamer assembly |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8016135/ https://www.ncbi.nlm.nih.gov/pubmed/33534950 http://dx.doi.org/10.1002/2211-5463.13106 |
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