The SARS coronavirus nucleocapsid protein--forms and functions.
Identifieur interne : 001546 ( Main/Exploration ); précédent : 001545; suivant : 001547The SARS coronavirus nucleocapsid protein--forms and functions.
Auteurs : Chung-Ke Chang [République populaire de Chine] ; Ming-Hon Hou [République populaire de Chine] ; Chi-Fon Chang [République populaire de Chine] ; Chwan-Deng Hsiao [République populaire de Chine] ; Tai-Huang Huang [République populaire de Chine]Source :
- Antiviral research [ 1872-9096 ] ; 2014.
Descripteurs français
- KwdFr :
- ARN viral (métabolisme), Assemblage viral, Conformation des protéines, Humains, Liaison aux protéines, Modèles biologiques, Modèles moléculaires, Phosphoprotéines (), Phosphoprotéines (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Structures macromoléculaires (ultrastructure), Virus du SRAS (), Virus du SRAS (physiologie).
- MESH :
- métabolisme : ARN viral, Phosphoprotéines, Protéines nucléocapside.
- physiologie : Virus du SRAS.
- ultrastructure : Structures macromoléculaires.
- Assemblage viral, Conformation des protéines, Humains, Liaison aux protéines, Modèles biologiques, Modèles moléculaires, Phosphoprotéines, Protéines nucléocapside, Virus du SRAS.
English descriptors
- KwdEn :
- Humans, Macromolecular Substances (ultrastructure), Models, Biological, Models, Molecular, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Phosphoproteins (chemistry), Phosphoproteins (metabolism), Protein Binding, Protein Conformation, RNA, Viral (metabolism), SARS Virus (chemistry), SARS Virus (physiology), Virus Assembly.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins, Phosphoproteins.
- chemical , metabolism : Nucleocapsid Proteins, Phosphoproteins, RNA, Viral.
- chemical , ultrastructure : Macromolecular Substances.
- chemistry : SARS Virus.
- physiology : SARS Virus.
- Humans, Models, Biological, Models, Molecular, Protein Binding, Protein Conformation, Virus Assembly.
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."
DOI: 10.1016/j.antiviral.2013.12.009
PubMed: 24418573
Affiliations:
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Electronic address: bmthh@ibms.sinica.edu.tw.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC; The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC; Department of Physics, National Taiwan Normal University, Taipei 11677, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antiviral research</title><idno type="eISSN">1872-9096</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Humans</term><term>Macromolecular Substances (ultrastructure)</term><term>Models, Biological</term><term>Models, Molecular</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Phosphoproteins (chemistry)</term><term>Phosphoproteins (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>RNA, Viral (metabolism)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (physiology)</term><term>Virus Assembly</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (métabolisme)</term><term>Assemblage viral</term><term>Conformation des protéines</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles biologiques</term><term>Modèles moléculaires</term><term>Phosphoprotéines ()</term><term>Phosphoprotéines (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (métabolisme)</term><term>Structures macromoléculaires (ultrastructure)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Phosphoproteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Phosphoproteins</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Macromolecular Substances</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Phosphoprotéines</term><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Structures macromoléculaires</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Models, Biological</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Assemblage viral</term><term>Conformation des protéines</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles biologiques</term><term>Modèles moléculaires</term><term>Phosphoprotéines</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name></noRegion><name sortKey="Chang, Chi Fon" sort="Chang, Chi Fon" uniqKey="Chang C" first="Chi-Fon" last="Chang">Chi-Fon Chang</name><name sortKey="Hou, Ming Hon" sort="Hou, Ming Hon" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name><name sortKey="Hsiao, Chwan Deng" sort="Hsiao, Chwan Deng" uniqKey="Hsiao C" first="Chwan-Deng" last="Hsiao">Chwan-Deng Hsiao</name><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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