SrasV1, PascalFrancis, Corpus, bibRecord, 000136

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

Identifieur interne : 000136 ( PascalFrancis/Corpus ); précédent : 000135; suivant : 000137

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

Auteurs : YONGJIN WANG ; HUILING SHI ; Pascal Rigolet ; NANNAN WU ; LICHEN ZHU ; Xu-Guang Xi ; Astrid Vabret ; XIAOMING WANG ; TIANHOU WANG

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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Format Inist (serveur)

NO :	PASCAL 10-0456478 INIST
ET :	Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities
AU :	YONGJIN WANG; HUILING SHI; RIGOLET (Pascal); NANNAN WU; LICHEN ZHU; XI (Xu-Guang); VABRET (Astrid); XIAOMING WANG; TIANHOU WANG
AF :	Laboratory of Wildlife Epidemic Diseases, East China Normal University/Shanghai 200062/Chine (1 aut., 2 aut., 4 aut., 5 aut., 8 aut., 9 aut.); CNRS, UMR 3348, Institut Curie-Section de Recherche, Centre Universitaire, Batiment 110/91405 Orsay/France (3 aut., 6 aut.); Laboratory of Virology, University Hospital of Caen, Avenue Georges Clemenceau/14033 Caen/France (7 aut.)
DT :	Publication en série; Papier de recherche; Niveau analytique
SO :	Infection, genetics and evolution : (Print); ISSN 1567-1348; Royaume-Uni; Da. 2010; Vol. 10; No. 7; Pp. 919-924; Bibl. 3/4 p.
LA :	Anglais
EA :	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.
CC :	002B05A02; 002B05C02C
FD :	Syndrome respiratoire aigu sévère; Protéine; Immunité; Coronavirus; Epidémiologie moléculaire
FG :	Virose; Infection; Coronaviridae; Nidovirales; Virus; Pathologie de l'appareil respiratoire; Pathologie des poumons
ED :	Severe acute respiratory syndrome; Protein; Immunity; Coronavirus; Molecular epidemiology
EG :	Viral disease; Infection; Coronaviridae; Nidovirales; Virus; Respiratory disease; Lung disease
SD :	Síndrome respiratorio agudo severo; Proteína; Inmunidad; Coronavirus; Epidemiología molecular
LO :	INIST-28039.354000191291300090
ID :	10-0456478

Links to Exploration step

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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<fA11 i1="09" i2="1"><s1>TIANHOU WANG</s1>
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<fA14 i1="01"><s1>Laboratory of Wildlife Epidemic Diseases, East China Normal University</s1>
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<server><NO>PASCAL 10-0456478 INIST</NO>
<ET>Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities</ET>
<AU>YONGJIN WANG; HUILING SHI; RIGOLET (Pascal); NANNAN WU; LICHEN ZHU; XI (Xu-Guang); VABRET (Astrid); XIAOMING WANG; TIANHOU WANG</AU>
<AF>Laboratory of Wildlife Epidemic Diseases, East China Normal University/Shanghai 200062/Chine (1 aut., 2 aut., 4 aut., 5 aut., 8 aut., 9 aut.); CNRS, UMR 3348, Institut Curie-Section de Recherche, Centre Universitaire, Batiment 110/91405 Orsay/France (3 aut., 6 aut.); Laboratory of Virology, University Hospital of Caen, Avenue Georges Clemenceau/14033 Caen/France (7 aut.)</AF>
<DT>Publication en série; Papier de recherche; Niveau analytique</DT>
<SO>Infection, genetics and evolution : (Print); ISSN 1567-1348; Royaume-Uni; Da. 2010; Vol. 10; No. 7; Pp. 919-924; Bibl. 3/4 p.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
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<ED>Severe acute respiratory syndrome; Protein; Immunity; Coronavirus; Molecular epidemiology</ED>
<EG>Viral disease; Infection; Coronaviridae; Nidovirales; Virus; Respiratory disease; Lung disease</EG>
<SD>Síndrome respiratorio agudo severo; Proteína; Inmunidad; Coronavirus; Epidemiología molecular</SD>
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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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