Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities
Identifieur interne : 000C06 ( Pmc/Checkpoint ); précédent : 000C05; suivant : 000C07Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities
Auteurs : Yongjin Wang [République populaire de Chine] ; Huiling Shi [République populaire de Chine] ; Pascal Rigolet [France] ; Nannan Wu [République populaire de Chine] ; Lichen Zhu [République populaire de Chine] ; Xu-Guang Xi [France] ; Astrid Vabret [France] ; Xiaoming Wang [République populaire de Chine] ; Tianhou Wang [République populaire de Chine]Source :
- Infection, Genetics and Evolution [ 1567-1348 ] ; 2010.
Abstract
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.
Url:
DOI: 10.1016/j.meegid.2010.05.014
PubMed: 20609418
PubMed Central: 7106014
Affiliations:
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<front><div type="abstract" xml:lang="en"><p>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.</p>
</div>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Infect Genet Evol</journal-id>
<journal-id journal-id-type="iso-abbrev">Infect. Genet. Evol</journal-id>
<journal-title-group><journal-title>Infection, Genetics and Evolution</journal-title>
</journal-title-group>
<issn pub-type="ppub">1567-1348</issn>
<issn pub-type="epub">1567-7257</issn>
<publisher><publisher-name>Elsevier B.V.</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">20609418</article-id>
<article-id pub-id-type="pmc">7106014</article-id>
<article-id pub-id-type="publisher-id">S1567-1348(10)00137-1</article-id>
<article-id pub-id-type="doi">10.1016/j.meegid.2010.05.014</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Yongjin</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Shi</surname>
<given-names>Huiling</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Rigolet</surname>
<given-names>Pascal</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wu</surname>
<given-names>Nannan</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zhu</surname>
<given-names>Lichen</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Xi</surname>
<given-names>Xu-Guang</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Vabret</surname>
<given-names>Astrid</given-names>
</name>
<xref rid="aff3" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Xiaoming</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wang</surname>
<given-names>Tianhou</given-names>
</name>
<email>thwang@bio.ecnu.edu.cn</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>a</label>
Laboratory of Wildlife Epidemic Diseases, East China Normal University, Shanghai 200062, China</aff>
<aff id="aff2"><label>b</label>
CNRS, UMR 3348, Institut Curie-Section de Recherche, Centre Universitaire, Batiment 110, F-91405 Orsay, France</aff>
<aff id="aff3"><label>c</label>
Laboratory of Virology, University Hospital of Caen, Avenue Georges Clemenceau, 14033 Caen cedex, France</aff>
<author-notes><corresp id="cor1"><label>⁎</label>
Corresponding author. Tel.: +86 21 6223 3012; fax: +86 21 6223 3012. <email>thwang@bio.ecnu.edu.cn</email>
</corresp>
<fn id="fn1"><label>1</label>
<p>These authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release"><day>2</day>
<month>6</month>
<year>2010</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>10</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="epub"><day>2</day>
<month>6</month>
<year>2010</year>
</pub-date>
<volume>10</volume>
<issue>7</issue>
<fpage>919</fpage>
<lpage>924</lpage>
<history><date date-type="received"><day>1</day>
<month>4</month>
<year>2010</year>
</date>
<date date-type="rev-recd"><day>24</day>
<month>5</month>
<year>2010</year>
</date>
<date date-type="accepted"><day>25</day>
<month>5</month>
<year>2010</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2010 Elsevier B.V. All rights reserved.</copyright-statement>
<copyright-year>2010</copyright-year>
<copyright-holder>Elsevier B.V.</copyright-holder>
<license><license-p>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.</license-p>
</license>
</permissions>
<abstract><p>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.</p>
</abstract>
<kwd-group><title>Keywords</title>
<kwd>Group I coronavirus</kwd>
<kwd>nsp1</kwd>
<kwd>Innate immunity</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>France</li>
<li>République populaire de Chine</li>
</country>
<region><li>Basse-Normandie</li>
<li>Région Normandie</li>
<li>Île-de-France</li>
</region>
<settlement><li>Caen</li>
<li>Orsay</li>
</settlement>
</list>
<tree><country name="République populaire de Chine"><noRegion><name sortKey="Wang, Yongjin" sort="Wang, Yongjin" uniqKey="Wang Y" first="Yongjin" last="Wang">Yongjin Wang</name>
</noRegion>
<name sortKey="Shi, Huiling" sort="Shi, Huiling" uniqKey="Shi H" first="Huiling" last="Shi">Huiling Shi</name>
<name sortKey="Wang, Tianhou" sort="Wang, Tianhou" uniqKey="Wang T" first="Tianhou" last="Wang">Tianhou Wang</name>
<name sortKey="Wang, Xiaoming" sort="Wang, Xiaoming" uniqKey="Wang X" first="Xiaoming" last="Wang">Xiaoming Wang</name>
<name sortKey="Wu, Nannan" sort="Wu, Nannan" uniqKey="Wu N" first="Nannan" last="Wu">Nannan Wu</name>
<name sortKey="Zhu, Lichen" sort="Zhu, Lichen" uniqKey="Zhu L" first="Lichen" last="Zhu">Lichen Zhu</name>
</country>
<country name="France"><region name="Île-de-France"><name sortKey="Rigolet, Pascal" sort="Rigolet, Pascal" uniqKey="Rigolet P" first="Pascal" last="Rigolet">Pascal Rigolet</name>
</region>
<name sortKey="Vabret, Astrid" sort="Vabret, Astrid" uniqKey="Vabret A" first="Astrid" last="Vabret">Astrid Vabret</name>
<name sortKey="Xi, Xu Guang" sort="Xi, Xu Guang" uniqKey="Xi X" first="Xu-Guang" last="Xi">Xu-Guang Xi</name>
</country>
</tree>
</affiliations>
</record>
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