Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
Identifieur interne : 000763 ( Pmc/Checkpoint ); précédent : 000762; suivant : 000764Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
Auteurs : Jian Lei [Allemagne] ; Yuri Kusov [Allemagne] ; Rolf Hilgenfeld [Allemagne]Source :
- Antiviral Research [ 0166-3542 ] ; 2017.
Abstract
The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called “hypervariable region”), a macrodomain (also named “X domain”), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2pro), the Nsp3 ectodomain (3Ecto, also called “zinc-finger domain”), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.
Url:
DOI: 10.1016/j.antiviral.2017.11.001
PubMed: 29128390
PubMed Central: 7113668
Affiliations:
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PMC:7113668Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called “hypervariable region”), a macrodomain (also named “X domain”), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2<sup>pro</sup>
), the Nsp3 ectodomain (3Ecto, also called “zinc-finger domain”), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.</p>
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<pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<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">29128390</article-id>
<article-id pub-id-type="pmc">7113668</article-id>
<article-id pub-id-type="publisher-id">S0166-3542(17)30397-2</article-id>
<article-id pub-id-type="doi">10.1016/j.antiviral.2017.11.001</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" id="au1"><name><surname>Lei</surname>
<given-names>Jian</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au2"><name><surname>Kusov</surname>
<given-names>Yuri</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au3"><name><surname>Hilgenfeld</surname>
<given-names>Rolf</given-names>
</name>
<email>hilgenfeld@biochem.uni-luebeck.de</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="cor1" ref-type="corresp">∗</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>a</label>
Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany</aff>
<aff id="aff2"><label>b</label>
German Center for Infection Research (DZIF), Hamburg – Lübeck – Borstel – Riems Site, University of Lübeck, Germany</aff>
<author-notes><corresp id="cor1"><label>∗</label>
Corresponding author. Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany. <email>hilgenfeld@biochem.uni-luebeck.de</email>
</corresp>
</author-notes>
<pub-date pub-type="pmc-release"><day>8</day>
<month>11</month>
<year>2017</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>1</month>
<year>2018</year>
</pub-date>
<pub-date pub-type="epub"><day>8</day>
<month>11</month>
<year>2017</year>
</pub-date>
<volume>149</volume>
<fpage>58</fpage>
<lpage>74</lpage>
<history><date date-type="received"><day>24</day>
<month>5</month>
<year>2017</year>
</date>
<date date-type="rev-recd"><day>29</day>
<month>10</month>
<year>2017</year>
</date>
<date date-type="accepted"><day>2</day>
<month>11</month>
<year>2017</year>
</date>
</history>
<permissions><copyright-statement>© 2017 Elsevier B.V. All rights reserved.</copyright-statement>
<copyright-year>2017</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 id="abs0010"><p>The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called “hypervariable region”), a macrodomain (also named “X domain”), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2<sup>pro</sup>
), the Nsp3 ectodomain (3Ecto, also called “zinc-finger domain”), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.</p>
</abstract>
<abstract abstract-type="author-highlights" id="abs0015"><title>Highlights</title>
<p><list list-type="simple" id="ulist0010"><list-item id="u0010"><label>•</label>
<p id="p0010">Nonstructural protein 3 (∼200 kD) is a multifunctional protein comprising up to 16 different domains and regions.</p>
</list-item>
<list-item id="u0015"><label>•</label>
<p id="p0015">Nsp3 binds to viral RNA, nucleocapsid protein, as well as other viral proteins, and participates in polyprotein processing.</p>
</list-item>
<list-item id="u0030"><label>•</label>
<p id="p0030">The papain-like protease of Nsp3 is an established target for new antivirals.</p>
</list-item>
<list-item id="u0020"><label>•</label>
<p id="p0020">Through its de-ADP-ribosylating, de-ubiquitinating, and de-ISGylating activities, Nsp3 counteracts host innate immunity.</p>
</list-item>
<list-item id="u0025"><label>•</label>
<p id="p0025">Structural data are available for the N-terminal two thirds of Nsp3, but domains in the remainder are poorly characterized.</p>
</list-item>
</list>
</p>
</abstract>
<kwd-group id="kwrds0010"><title>Keywords</title>
<kwd>Ubiquitin-like domain</kwd>
<kwd>Papain-like protease</kwd>
<kwd>Macrodomain</kwd>
<kwd>Nucleic-acid binding domain</kwd>
<kwd>Innate immunity</kwd>
<kwd>Structural biology</kwd>
</kwd-group>
<kwd-group id="kwrds0015"><title>Abbreviations</title>
<kwd>3CL<sup>pro</sup>
, 3C-like protease</kwd>
<kwd>3Ecto, Nsp3 ectodomain</kwd>
<kwd>ADPr, ADP-ribose</kwd>
<kwd>ADRP, ADP-ribose-1″-phosphate phosphatase</kwd>
<kwd>ARTD, ADP-ribosyltransferases diphtheria toxin-like</kwd>
<kwd>βSM, betacoronavirus-specific marker</kwd>
<kwd>CHIKV, Chikungunya virus</kwd>
<kwd>CM, convoluted membrane</kwd>
<kwd>CoV, coronavirus</kwd>
<kwd>DMV, double-membrane vesicle</kwd>
<kwd>DPUP, Domain Preceding Ubl2 and PL2<sup>pro</sup>
</kwd>
<kwd>DUB, deubiquitinating</kwd>
<kwd>ER, Endoplasmic Reticulum</kwd>
<kwd>GST, glutathione S-transferase</kwd>
<kwd>hISG15, human interferon-stimulated gene 15</kwd>
<kwd>HCoV, human coronavirus</kwd>
<kwd>HEV, hepatitis E virus</kwd>
<kwd>HKU, Hong Kong University</kwd>
<kwd>HVR, hypervariable region</kwd>
<kwd>IBV, infectious bronchitis virus</kwd>
<kwd>IFN, interferon</kwd>
<kwd>IL-6, Interleukin 6</kwd>
<kwd>IRF, interferon regulatory factor</kwd>
<kwd>mISG15, mouse interferon-stimulated gene 15</kwd>
<kwd>M<sup>pro</sup>
, main protease</kwd>
<kwd>Mac, macrodomain</kwd>
<kwd>MARylation, mono-ADP-ribosylation</kwd>
<kwd>MDM2, mouse double minute 2 homolog</kwd>
<kwd>MERS, Middle-East respiratory syndrome</kwd>
<kwd>MHV, mouse hepatitis virus</kwd>
<kwd>MKRN, makorin ring finger protein</kwd>
<kwd>N, nucleocapsid</kwd>
<kwd>NAB, nucleic-acid binding domain</kwd>
<kwd>NF-κB, nuclear factor kappa-light-chain-enhancer of activated B cells</kwd>
<kwd>Nsp, non-structural protein</kwd>
<kwd>NTD, N-terminal domain</kwd>
<kwd>ORF, open reading frame</kwd>
<kwd>PABP, poly(A)-binding protein</kwd>
<kwd>PARP, poly(ADP-ribose) polymerase</kwd>
<kwd>PARylation, poly-ADP-ribosylation</kwd>
<kwd>RCHY1, RING finger and CHY zinc-finger domain-containing protein 1</kwd>
<kwd>RID, Ras-interacting domain</kwd>
<kwd>PL<sup>pro</sup>
, papain-like protease</kwd>
<kwd>R.M.S.D., root-mean-square deviation</kwd>
<kwd>RTC, replication/transcription complex</kwd>
<kwd>SARS, severe acute respiratory syndrome</kwd>
<kwd>SUD, SARS-unique domain</kwd>
<kwd>TGEV, transmissible gastroenteritis virus</kwd>
<kwd>TM, transmembrane</kwd>
<kwd>TNF, tumor necrosis factor</kwd>
<kwd>TRS, transcriptional regulatory sequence</kwd>
<kwd>Ubl, ubiquitin-like</kwd>
<kwd>Ub, ubiquitin</kwd>
<kwd>USP, ubiquitin-specific protease</kwd>
<kwd>UTR, untranslated region</kwd>
<kwd>VEEV, Venezuelan equine encephalitis virus</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Allemagne</li>
</country>
</list>
<tree><country name="Allemagne"><noRegion><name sortKey="Lei, Jian" sort="Lei, Jian" uniqKey="Lei J" first="Jian" last="Lei">Jian Lei</name>
</noRegion>
<name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name>
<name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name>
<name sortKey="Kusov, Yuri" sort="Kusov, Yuri" uniqKey="Kusov Y" first="Yuri" last="Kusov">Yuri Kusov</name>
</country>
</tree>
</affiliations>
</record>
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