SrasV1, PascalFrancis, Curation, bibRecord, 000852

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

Identifieur interne : 000852 ( PascalFrancis/Curation ); précédent : 000851; suivant : 000853

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 :

Infection, genetics and evolution : (Print) [ 1567-1348 ] ; 2010.

RBID : Pascal:10-0456478

Descripteurs français

Pascal (Inist)
- Syndrome respiratoire aigu sévère, Protéine, Immunité, Coronavirus, Epidémiologie moléculaire.

English descriptors

KwdEn :
- Coronavirus, Immunity, Molecular epidemiology, Protein, Severe acute respiratory syndrome.

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 1 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.

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C01	`01`		`ENG`	@0 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 1 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.
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Pascal:10-0456478

Le document en format XML

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<front><div type="abstract" xml:lang="en">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 1 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.</div>
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<s3>PR</s3>
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<fA61><s0>A</s0>
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<fA64 i1="01" i2="1"><s0>Infection, genetics and evolution : (Print)</s0>
</fA64>
<fA66 i1="01"><s0>GBR</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>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 1 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.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002B05A02</s0>
</fC02>
<fC02 i1="02" i2="X"><s0>002B05C02C</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0>
<s2>NM</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0>
<s2>NM</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0>
<s2>NM</s2>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Protéine</s0>
<s5>07</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Protein</s0>
<s5>07</s5>
</fC03>
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<s5>07</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Immunité</s0>
<s5>08</s5>
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<s5>08</s5>
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<s5>08</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>10</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>10</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>10</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Epidémiologie moléculaire</s0>
<s5>31</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Molecular epidemiology</s0>
<s5>31</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Epidemiología molecular</s0>
<s5>31</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Virose</s0>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Viral disease</s0>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Virosis</s0>
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<fC07 i1="02" i2="X" l="FRE"><s0>Infection</s0>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Infection</s0>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Infección</s0>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Pathologie de l'appareil respiratoire</s0>
<s5>38</s5>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Respiratory disease</s0>
<s5>38</s5>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0>
<s5>38</s5>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Pathologie des poumons</s0>
<s5>39</s5>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Lung disease</s0>
<s5>39</s5>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Pulmón patología</s0>
<s5>39</s5>
</fC07>
<fN21><s1>298</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
</inist>
</record>

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

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

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