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Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities

Identifieur interne : 000215 ( France/Analysis ); précédent : 000214; suivant : 000216

Nsp1 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 :

RBID : PMC:7106014

Descripteurs français

English descriptors

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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PMC:7106014

Le document en format XML

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<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>
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</back>
</TEI>
<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">
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<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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