SrasV1, Main, Exploration, bibRecord, 001782

The SARS coronavirus nucleocapsid protein - Forms and functions

Identifieur interne : 001782 ( Main/Exploration ); précédent : 001781; suivant : 001783

The SARS coronavirus nucleocapsid protein - Forms and functions

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

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.".

Affiliations:

Taïwan

Links toward previous steps (curation, corpus...)

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to stream PascalFrancis, to step Curation: 000979
to stream PascalFrancis, to step Checkpoint: 000001
to stream Main, to step Merge: 001788
to stream Main, to step Curation: 001782

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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The SARS coronavirus nucleocapsid protein - Forms and functions

The SARS coronavirus nucleocapsid protein - Forms and functions

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri