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Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities
The nsp1 protein of the highly pathogenic SARS coronavirus suppresses host protein synthesis, including genes involved in the innate immune system. A bioinformatic analysis revealed that the nsp1 proteins of group I and SARS coronaviruses have similar structures. Nsp1 proteins of group I coronavirus...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7106014/ https://www.ncbi.nlm.nih.gov/pubmed/20609418 http://dx.doi.org/10.1016/j.meegid.2010.05.014 |
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author | Wang, Yongjin Shi, Huiling Rigolet, Pascal Wu, Nannan Zhu, Lichen Xi, Xu-Guang Vabret, Astrid Wang, Xiaoming Wang, Tianhou |
author_facet | Wang, Yongjin Shi, Huiling Rigolet, Pascal Wu, Nannan Zhu, Lichen Xi, Xu-Guang Vabret, Astrid Wang, Xiaoming Wang, Tianhou |
author_sort | Wang, Yongjin |
collection | PubMed |
description | The nsp1 protein of the highly pathogenic SARS coronavirus suppresses host protein synthesis, including genes involved in the innate immune system. A bioinformatic analysis revealed that the nsp1 proteins of group I and SARS coronaviruses have similar structures. Nsp1 proteins of group I coronaviruses interacted with host ribosomal 40S subunit and did not inhibit IRF-3 activation. However, synthesis of host immune and non-immune proteins was inhibited by nsp1 proteins at both transcriptional and translational levels, similar to SARS coronavirus nsp1. These results indicate that different coronaviruses might employ the same nsp1 mechanism to antagonize host innate immunity and cell proliferation. However, nsp1 may not be the key determinant of viral pathogenicity, or the factor used by the SARS coronavirus to evade host innate immunity. |
format | Online Article Text |
id | pubmed-7106014 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71060142020-03-31 Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities Wang, Yongjin Shi, Huiling Rigolet, Pascal Wu, Nannan Zhu, Lichen Xi, Xu-Guang Vabret, Astrid Wang, Xiaoming Wang, Tianhou Infect Genet Evol Article The nsp1 protein of the highly pathogenic SARS coronavirus suppresses host protein synthesis, including genes involved in the innate immune system. A bioinformatic analysis revealed that the nsp1 proteins of group I and SARS coronaviruses have similar structures. Nsp1 proteins of group I coronaviruses interacted with host ribosomal 40S subunit and did not inhibit IRF-3 activation. However, synthesis of host immune and non-immune proteins was inhibited by nsp1 proteins at both transcriptional and translational levels, similar to SARS coronavirus nsp1. These results indicate that different coronaviruses might employ the same nsp1 mechanism to antagonize host innate immunity and cell proliferation. However, nsp1 may not be the key determinant of viral pathogenicity, or the factor used by the SARS coronavirus to evade host innate immunity. Elsevier B.V. 2010-10 2010-06-02 /pmc/articles/PMC7106014/ /pubmed/20609418 http://dx.doi.org/10.1016/j.meegid.2010.05.014 Text en Copyright © 2010 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Wang, Yongjin Shi, Huiling Rigolet, Pascal Wu, Nannan Zhu, Lichen Xi, Xu-Guang Vabret, Astrid Wang, Xiaoming Wang, Tianhou Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities |
title | Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities |
title_full | Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities |
title_fullStr | Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities |
title_full_unstemmed | Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities |
title_short | Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities |
title_sort | nsp1 proteins of group i and sars coronaviruses share structural and functional similarities |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7106014/ https://www.ncbi.nlm.nih.gov/pubmed/20609418 http://dx.doi.org/10.1016/j.meegid.2010.05.014 |
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