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I(nsp1)ecting SARS-CoV-2–ribosome interactions

While SARS-CoV-2 is causing modern human history’s most serious health crisis and upending our way of life, clinical and basic research on the virus is advancing rapidly, leading to fascinating discoveries. Two studies have revealed how the viral virulence factor, nonstructural protein 1 (Nsp1), bin...

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Autores principales: Simeoni, Matthieu, Cavinato, Théo, Rodriguez, Daniel, Gatfield, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8192748/
https://www.ncbi.nlm.nih.gov/pubmed/34112887
http://dx.doi.org/10.1038/s42003-021-02265-0
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author Simeoni, Matthieu
Cavinato, Théo
Rodriguez, Daniel
Gatfield, David
author_facet Simeoni, Matthieu
Cavinato, Théo
Rodriguez, Daniel
Gatfield, David
author_sort Simeoni, Matthieu
collection PubMed
description While SARS-CoV-2 is causing modern human history’s most serious health crisis and upending our way of life, clinical and basic research on the virus is advancing rapidly, leading to fascinating discoveries. Two studies have revealed how the viral virulence factor, nonstructural protein 1 (Nsp1), binds human ribosomes to inhibit host cell translation. Here, we examine the main conclusions on the molecular activity of Nsp1 and its role in suppressing innate immune responses. We discuss different scenarios potentially explaining how the viral RNA can bypass its own translation blockage and speculate on the suitability of Nsp1 as a therapeutic target.
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spelling pubmed-81927482021-06-17 I(nsp1)ecting SARS-CoV-2–ribosome interactions Simeoni, Matthieu Cavinato, Théo Rodriguez, Daniel Gatfield, David Commun Biol Perspective While SARS-CoV-2 is causing modern human history’s most serious health crisis and upending our way of life, clinical and basic research on the virus is advancing rapidly, leading to fascinating discoveries. Two studies have revealed how the viral virulence factor, nonstructural protein 1 (Nsp1), binds human ribosomes to inhibit host cell translation. Here, we examine the main conclusions on the molecular activity of Nsp1 and its role in suppressing innate immune responses. We discuss different scenarios potentially explaining how the viral RNA can bypass its own translation blockage and speculate on the suitability of Nsp1 as a therapeutic target. Nature Publishing Group UK 2021-06-10 /pmc/articles/PMC8192748/ /pubmed/34112887 http://dx.doi.org/10.1038/s42003-021-02265-0 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Perspective
Simeoni, Matthieu
Cavinato, Théo
Rodriguez, Daniel
Gatfield, David
I(nsp1)ecting SARS-CoV-2–ribosome interactions
title I(nsp1)ecting SARS-CoV-2–ribosome interactions
title_full I(nsp1)ecting SARS-CoV-2–ribosome interactions
title_fullStr I(nsp1)ecting SARS-CoV-2–ribosome interactions
title_full_unstemmed I(nsp1)ecting SARS-CoV-2–ribosome interactions
title_short I(nsp1)ecting SARS-CoV-2–ribosome interactions
title_sort i(nsp1)ecting sars-cov-2–ribosome interactions
topic Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8192748/
https://www.ncbi.nlm.nih.gov/pubmed/34112887
http://dx.doi.org/10.1038/s42003-021-02265-0
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