SrasV1, PascalFrancis, Corpus, bibRecord, 000008

The SARS coronavirus nucleocapsid protein - Forms and functions

Identifieur interne : 000008 ( PascalFrancis/Corpus ); précédent : 000007; suivant : 000009

The SARS coronavirus nucleocapsid protein - Forms and functions

Auteurs : Chung-Ke Chang ; Ming-Hon Hou ; Chi-Fon Chang ; Chwan-Deng Hsiao ; Tai-Huang Huang

Source :

Antiviral research [ 0166-3542 ] ; 2014.

RBID : Pascal:14-0119194

Descripteurs français

Pascal (Inist)
- Virus syndrome respiratoire aigu sévère, Nucléocapside, Protéine, Syndrome respiratoire aigu sévère, Capside, Encapsidation, Désordre, Ribonucléoprotéine.

English descriptors

KwdEn :
- Capsid, Disorder, Encapsidation, Nucleocapsid, Protein, Ribonucleoprotein, Severe acute respiratory syndrome, Severe acute respiratory syndrome virus.

Abstract

The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.".

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A02	`01`			`@0 ARSRDR`
A03		`1`		`@0 Antivir. res.`
A05				`@2 103`
A08	`01`	`1`	`ENG`	`@1 The SARS coronavirus nucleocapsid protein - Forms and functions`
A11	`01`	`1`		`@1 CHANG (Chung-Ke)`
A11	`02`	`1`		`@1 HOU (Ming-Hon)`
A11	`03`	`1`		`@1 CHANG (Chi-Fon)`
A11	`04`	`1`		`@1 HSIAO (Chwan-Deng)`
A11	`05`	`1`		`@1 HUANG (Tai-Huang)`
A14	`01`			`@1 Institute of Biomedical Sciences, Academia Sinica @2 Taipei 11529 @3 TWN @Z 1 aut. @Z 5 aut.`
A14	`02`			`@1 Department of Life Science, National Chung Hsing University @2 Taichung 40254 @3 TWN @Z 2 aut.`
A14	`03`			`@1 The Genomics Research Center, Academia Sinica @2 Taipei 11529 @3 TWN @Z 3 aut. @Z 5 aut.`
A14	`04`			`@1 Institute of Molecular Biology, Academia Sinica @2 Taipei 11529 @3 TWN @Z 4 aut.`
A14	`05`			`@1 Department of Physics, National Taiwan Normal University @2 Taipei 11677 @3 TWN @Z 5 aut.`
A20				`@1 39-50`
A21				`@1 2014`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 18839 @5 354000506167970060`
A44				`@0 0000 @1 © 2014 INIST-CNRS. All rights reserved.`
A45				`@0 1 p.3/4`
A47	`01`	`1`		`@0 14-0119194`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Antiviral research`
A66	`01`			`@0 GBR`
C01	`01`		`ENG`	@0 The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.".
C02	`01`	`X`		`@0 002B02S05`
C02	`02`	`X`		`@0 002B05C02C`
C03	`01`	`X`	`FRE`	`@0 Virus syndrome respiratoire aigu sévère @2 NW @5 01`
C03	`01`	`X`	`ENG`	`@0 Severe acute respiratory syndrome virus @2 NW @5 01`
C03	`01`	`X`	`SPA`	`@0 Severe acute respiratory syndrome virus @2 NW @5 01`
C03	`02`	`X`	`FRE`	`@0 Nucléocapside @5 02`
C03	`02`	`X`	`ENG`	`@0 Nucleocapsid @5 02`
C03	`02`	`X`	`SPA`	`@0 Nucleocápside @5 02`
C03	`03`	`X`	`FRE`	`@0 Protéine @5 03`
C03	`03`	`X`	`ENG`	`@0 Protein @5 03`
C03	`03`	`X`	`SPA`	`@0 Proteína @5 03`
C03	`04`	`X`	`FRE`	`@0 Syndrome respiratoire aigu sévère @2 NM @5 05`
C03	`04`	`X`	`ENG`	`@0 Severe acute respiratory syndrome @2 NM @5 05`
C03	`04`	`X`	`SPA`	`@0 Síndrome respiratorio agudo severo @2 NM @5 05`
C03	`05`	`X`	`FRE`	`@0 Capside @5 07`
C03	`05`	`X`	`ENG`	`@0 Capsid @5 07`
C03	`05`	`X`	`SPA`	`@0 Cápside @5 07`
C03	`06`	`X`	`FRE`	`@0 Encapsidation @5 08`
C03	`06`	`X`	`ENG`	`@0 Encapsidation @5 08`
C03	`06`	`X`	`SPA`	`@0 Encapsidación @5 08`
C03	`07`	`X`	`FRE`	`@0 Désordre @5 09`
C03	`07`	`X`	`ENG`	`@0 Disorder @5 09`
C03	`07`	`X`	`SPA`	`@0 Desorden @5 09`
C03	`08`	`X`	`FRE`	`@0 Ribonucléoprotéine @5 10`
C03	`08`	`X`	`ENG`	`@0 Ribonucleoprotein @5 10`
C03	`08`	`X`	`SPA`	`@0 Ribonucleoproteina @5 10`
C07	`01`	`X`	`FRE`	`@0 Coronavirus @2 NW`
C07	`01`	`X`	`ENG`	`@0 Coronavirus @2 NW`
C07	`01`	`X`	`SPA`	`@0 Coronavirus @2 NW`
C07	`02`	`X`	`FRE`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`SPA`	`@0 Coronaviridae @2 NW`
C07	`03`	`X`	`FRE`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`ENG`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`SPA`	`@0 Nidovirales @2 NW`
C07	`04`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`04`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`04`	`X`	`SPA`	`@0 Virus @2 NW`
C07	`05`	`X`	`FRE`	`@0 Virose`
C07	`05`	`X`	`ENG`	`@0 Viral disease`
C07	`05`	`X`	`SPA`	`@0 Virosis`
C07	`06`	`X`	`FRE`	`@0 Infection`
C07	`06`	`X`	`ENG`	`@0 Infection`
C07	`06`	`X`	`SPA`	`@0 Infección`
C07	`07`	`X`	`FRE`	`@0 Pathologie de l'appareil respiratoire @5 37`
C07	`07`	`X`	`ENG`	`@0 Respiratory disease @5 37`
C07	`07`	`X`	`SPA`	`@0 Aparato respiratorio patología @5 37`
C07	`08`	`X`	`FRE`	`@0 Pathologie des poumons @5 38`
C07	`08`	`X`	`ENG`	`@0 Lung disease @5 38`
C07	`08`	`X`	`SPA`	`@0 Pulmón patología @5 38`
N21				`@1 153`

Format Inist (serveur)

NO :	PASCAL 14-0119194 INIST
ET :	The SARS coronavirus nucleocapsid protein - Forms and functions
AU :	CHANG (Chung-Ke); HOU (Ming-Hon); CHANG (Chi-Fon); HSIAO (Chwan-Deng); HUANG (Tai-Huang)
AF :	Institute of Biomedical Sciences, Academia Sinica/Taipei 11529/Taïwan (1 aut., 5 aut.); Department of Life Science, National Chung Hsing University/Taichung 40254/Taïwan (2 aut.); The Genomics Research Center, Academia Sinica/Taipei 11529/Taïwan (3 aut., 5 aut.); Institute of Molecular Biology, Academia Sinica/Taipei 11529/Taïwan (4 aut.); Department of Physics, National Taiwan Normal University/Taipei 11677/Taïwan (5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2014; Vol. 103; Pp. 39-50; Bibl. 1 p.3/4
LA :	Anglais
EA :	The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.".
CC :	002B02S05; 002B05C02C
FD :	Virus syndrome respiratoire aigu sévère; Nucléocapside; Protéine; Syndrome respiratoire aigu sévère; Capside; Encapsidation; Désordre; Ribonucléoprotéine
FG :	Coronavirus; Coronaviridae; Nidovirales; Virus; Virose; Infection; Pathologie de l'appareil respiratoire; Pathologie des poumons
ED :	Severe acute respiratory syndrome virus; Nucleocapsid; Protein; Severe acute respiratory syndrome; Capsid; Encapsidation; Disorder; Ribonucleoprotein
EG :	Coronavirus; Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Respiratory disease; Lung disease
SD :	Severe acute respiratory syndrome virus; Nucleocápside; Proteína; Síndrome respiratorio agudo severo; Cápside; Encapsidación; Desorden; Ribonucleoproteina
LO :	INIST-18839.354000506167970060
ID :	14-0119194

Links to Exploration step

Pascal:14-0119194

Le document en format XML

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<front><div type="abstract" xml:lang="en">The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.".</div>
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</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Severe acute respiratory syndrome virus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
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<s5>07</s5>
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<s5>08</s5>
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<s5>09</s5>
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<s5>10</s5>
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<s5>10</s5>
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<s2>NW</s2>
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<fC07 i1="02" i2="X" l="SPA"><s0>Coronaviridae</s0>
<s2>NW</s2>
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<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
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<fC07 i1="04" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Virose</s0>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Viral disease</s0>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Virosis</s0>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Infection</s0>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Infection</s0>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Infección</s0>
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<fC07 i1="07" i2="X" l="FRE"><s0>Pathologie de l'appareil respiratoire</s0>
<s5>37</s5>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Respiratory disease</s0>
<s5>37</s5>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0>
<s5>37</s5>
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<fC07 i1="08" i2="X" l="FRE"><s0>Pathologie des poumons</s0>
<s5>38</s5>
</fC07>
<fC07 i1="08" i2="X" l="ENG"><s0>Lung disease</s0>
<s5>38</s5>
</fC07>
<fC07 i1="08" i2="X" l="SPA"><s0>Pulmón patología</s0>
<s5>38</s5>
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<fN21><s1>153</s1>
</fN21>
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<server><NO>PASCAL 14-0119194 INIST</NO>
<ET>The SARS coronavirus nucleocapsid protein - Forms and functions</ET>
<AU>CHANG (Chung-Ke); HOU (Ming-Hon); CHANG (Chi-Fon); HSIAO (Chwan-Deng); HUANG (Tai-Huang)</AU>
<AF>Institute of Biomedical Sciences, Academia Sinica/Taipei 11529/Taïwan (1 aut., 5 aut.); Department of Life Science, National Chung Hsing University/Taichung 40254/Taïwan (2 aut.); The Genomics Research Center, Academia Sinica/Taipei 11529/Taïwan (3 aut., 5 aut.); Institute of Molecular Biology, Academia Sinica/Taipei 11529/Taïwan (4 aut.); Department of Physics, National Taiwan Normal University/Taipei 11677/Taïwan (5 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2014; Vol. 103; Pp. 39-50; Bibl. 1 p.3/4</SO>
<LA>Anglais</LA>
<EA>The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.".</EA>
<CC>002B02S05; 002B05C02C</CC>
<FD>Virus syndrome respiratoire aigu sévère; Nucléocapside; Protéine; Syndrome respiratoire aigu sévère; Capside; Encapsidation; Désordre; Ribonucléoprotéine</FD>
<FG>Coronavirus; Coronaviridae; Nidovirales; Virus; Virose; Infection; Pathologie de l'appareil respiratoire; Pathologie des poumons</FG>
<ED>Severe acute respiratory syndrome virus; Nucleocapsid; Protein; Severe acute respiratory syndrome; Capsid; Encapsidation; Disorder; Ribonucleoprotein</ED>
<EG>Coronavirus; Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Respiratory disease; Lung disease</EG>
<SD>Severe acute respiratory syndrome virus; Nucleocápside; Proteína; Síndrome respiratorio agudo severo; Cápside; Encapsidación; Desorden; Ribonucleoproteina</SD>
<LO>INIST-18839.354000506167970060</LO>
<ID>14-0119194</ID>
</server>
</inist>
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The SARS coronavirus nucleocapsid protein - Forms and functions

The SARS coronavirus nucleocapsid protein - Forms and functions

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