The SARS coronavirus nucleocapsid protein – Forms and functions
Identifieur interne : 000F56 ( Pmc/Checkpoint ); précédent : 000F55; suivant : 000F57The 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 [ 0166-3542 ] ; 2014.
Abstract
Coronavirus N proteins share the same modular organization. Structures of SARS-CoV N protein provide insight into nucleocapsid formation. N protein binds to nucleic acid at multiple sites in a coupled-allostery manner. A RNP packaging model highlighting the importance of disorder and modularity is proposed.
Url:
DOI: 10.1016/j.antiviral.2013.12.009
PubMed: 24418573
PubMed Central: 7113676
Affiliations:
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PMC:7113676Le document en format XML
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Chine</country><wicri:regionArea>Department of Life Science, National Chung Hsing University, Taichung 40254, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author><author><name sortKey="Chang, Chi Fon" sort="Chang, Chi Fon" uniqKey="Chang C" first="Chi-Fon" last="Chang">Chi-Fon Chang</name><affiliation wicri:level="1"><nlm:aff id="af015">The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author><author><name sortKey="Hsiao, Chwan Deng" sort="Hsiao, Chwan Deng" uniqKey="Hsiao C" first="Chwan-Deng" last="Hsiao">Chwan-Deng Hsiao</name><affiliation wicri:level="1"><nlm:aff id="af020">Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" 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type="wicri:Area/Pmc/Curation">001278</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001278</idno><idno type="wicri:Area/Pmc/Checkpoint">000F56</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000F56</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The SARS coronavirus nucleocapsid protein – Forms and functions</title><author><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name><affiliation wicri:level="1"><nlm:aff id="af005">Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author><author><name sortKey="Hou, Ming Hon" sort="Hou, Ming Hon" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name><affiliation wicri:level="1"><nlm:aff id="af010">Department of Life Science, National Chung Hsing University, Taichung 40254, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>Department of Life Science, National Chung Hsing University, Taichung 40254, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author><author><name sortKey="Chang, Chi Fon" sort="Chang, Chi Fon" uniqKey="Chang C" first="Chi-Fon" last="Chang">Chi-Fon Chang</name><affiliation wicri:level="1"><nlm:aff id="af015">The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author><author><name sortKey="Hsiao, Chwan Deng" sort="Hsiao, Chwan Deng" uniqKey="Hsiao C" first="Chwan-Deng" last="Hsiao">Chwan-Deng Hsiao</name><affiliation wicri:level="1"><nlm:aff id="af020">Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation></author><author><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name><affiliation wicri:level="1"><nlm:aff id="af005">Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="af015">The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan</wicri:regionArea><wicri:noRegion>Taiwan</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="af025">Department of Physics, National Taiwan Normal University, Taipei 11677, Taiwan, ROC</nlm:aff><country xml:lang="fr" wicri:curation="lc">République populaire de Chine</country><wicri:regionArea>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="ISSN">0166-3542</idno><idno type="eISSN">1872-9096</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Highlights</title><p><list list-type="simple" id="l0005"><list-item id="o0005"><label>•</label><p id="p0145">Coronavirus N proteins share the same modular organization.</p></list-item><list-item id="o0010"><label>•</label><p id="p0150">Structures of SARS-CoV N protein provide insight into nucleocapsid formation.</p></list-item><list-item id="o0015"><label>•</label><p id="p0155">N protein binds to nucleic acid at multiple sites in a coupled-allostery manner.</p></list-item><list-item id="o0020"><label>•</label><p id="p0160">A RNP packaging model highlighting the importance of disorder and modularity is proposed.</p></list-item></list></p></div></front><back><div1 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Antiviral Res</journal-id><journal-id journal-id-type="iso-abbrev">Antiviral Res</journal-id><journal-title-group><journal-title>Antiviral Research</journal-title></journal-title-group><issn pub-type="ppub">0166-3542</issn><issn pub-type="epub">1872-9096</issn><publisher><publisher-name>Elsevier B.V.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">24418573</article-id><article-id pub-id-type="pmc">7113676</article-id><article-id pub-id-type="publisher-id">S0166-3542(13)00378-1</article-id><article-id pub-id-type="doi">10.1016/j.antiviral.2013.12.009</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The SARS coronavirus nucleocapsid protein – Forms and functions</article-title></title-group><contrib-group><contrib contrib-type="author" id="au005"><name><surname>Chang</surname><given-names>Chung-ke</given-names></name><xref rid="af005" ref-type="aff">a</xref></contrib><contrib contrib-type="author" id="au010"><name><surname>Hou</surname><given-names>Ming-Hon</given-names></name><xref rid="af010" ref-type="aff">b</xref></contrib><contrib contrib-type="author" id="au015"><name><surname>Chang</surname><given-names>Chi-Fon</given-names></name><xref rid="af015" ref-type="aff">c</xref></contrib><contrib contrib-type="author" id="au020"><name><surname>Hsiao</surname><given-names>Chwan-Deng</given-names></name><xref rid="af020" ref-type="aff">d</xref></contrib><contrib contrib-type="author" id="au025"><name><surname>Huang</surname><given-names>Tai-huang</given-names></name><email>bmthh@ibms.sinica.edu.tw</email><xref rid="af005" ref-type="aff">a</xref><xref rid="af015" ref-type="aff">c</xref><xref rid="af025" ref-type="aff">e</xref><xref rid="cor1" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="af005"><label>a</label>Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC</aff><aff id="af010"><label>b</label>Department of Life Science, National Chung Hsing University, Taichung 40254, Taiwan, ROC</aff><aff id="af015"><label>c</label>The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC</aff><aff id="af020"><label>d</label>Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC</aff><aff id="af025"><label>e</label>Department of Physics, National Taiwan Normal University, Taipei 11677, Taiwan, ROC</aff><author-notes><corresp id="cor1"><label>⁎</label>Corresponding author at: Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC. Tel.: +886 2 2652 3036; fax +886 2 2788 7641. <email>bmthh@ibms.sinica.edu.tw</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>11</day><month>1</month><year>2014</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>3</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>11</day><month>1</month><year>2014</year></pub-date><volume>103</volume><fpage>39</fpage><lpage>50</lpage><history><date date-type="received"><day>28</day><month>10</month><year>2013</year></date><date date-type="rev-recd"><day>8</day><month>12</month><year>2013</year></date><date date-type="accepted"><day>20</day><month>12</month><year>2013</year></date></history><permissions><copyright-statement>Copyright © 2014 Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2014</copyright-year><copyright-holder>Elsevier B.V.</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract abstract-type="author-highlights" id="ab005"><title>Highlights</title><p><list list-type="simple" id="l0005"><list-item id="o0005"><label>•</label><p id="p0145">Coronavirus N proteins share the same modular organization.</p></list-item><list-item id="o0010"><label>•</label><p id="p0150">Structures of SARS-CoV N protein provide insight into nucleocapsid formation.</p></list-item><list-item id="o0015"><label>•</label><p id="p0155">N protein binds to nucleic acid at multiple sites in a coupled-allostery manner.</p></list-item><list-item id="o0020"><label>•</label><p id="p0160">A RNP packaging model highlighting the importance of disorder and modularity is proposed.</p></list-item></list></p></abstract><abstract id="ab010"><p>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.”</p></abstract><kwd-group id="kg005"><title>Abbreviations</title><kwd>CTD, the C-terminal domain of N protein (a.a. 248–365)</kwd><kwd>DD, the di-domain comprising NTD, LKR and CTD (a.a. 45–365)</kwd><kwd>HCoV, human coronavirus</kwd><kwd>IDP, intrinsically disordered protein</kwd><kwd>IDR, intrinsically disordered region</kwd><kwd>LKR, the linker region of SARS-CoV N protein (a.a. 182–247)</kwd><kwd>N, nucleocapsid protein</kwd><kwd>NTD, the N-terminal domain of N protein (a.a. 45–181)</kwd><kwd>MHV, mouse hepatitis virus</kwd><kwd>RMSD, root mean square deviation</kwd><kwd>RNP, ribonucleoprotein</kwd><kwd>SARS-CoV, severe acute respiratory syndrome coronavirus</kwd></kwd-group><kwd-group id="kg010"><title>Keywords</title><kwd>SARS</kwd><kwd>Coronavirus</kwd><kwd>Nucleocapsid protein</kwd><kwd>Capsid packaging</kwd><kwd>Intrinsic disorder</kwd><kwd>RNP</kwd></kwd-group></article-meta></front></pmc><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><name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</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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