Variable Oligomerization Modes in Coronavirus Non-structural Protein 9
Identifieur interne : 000153 ( Ncbi/Merge ); précédent : 000152; suivant : 000154Variable Oligomerization Modes in Coronavirus Non-structural Protein 9
Auteurs : Rajesh Ponnusamy [Allemagne] ; Ralf Moll [Allemagne] ; Thomas Weimar [Allemagne] ; Jeroen R. Mesters [Allemagne] ; Rolf Hilgenfeld [Allemagne]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 2008.
Abstract
Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.
Url:
DOI: 10.1016/j.jmb.2008.07.071
PubMed: 18694760
PubMed Central: 7094590
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<front><div type="abstract" xml:lang="en"><p>Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.</p>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Mol Biol</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Mol. Biol</journal-id>
<journal-title-group><journal-title>Journal of Molecular Biology</journal-title>
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<issn pub-type="ppub">0022-2836</issn>
<issn pub-type="epub">1089-8638</issn>
<publisher><publisher-name>Elsevier</publisher-name>
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<article-meta><article-id pub-id-type="pmid">18694760</article-id>
<article-id pub-id-type="pmc">7094590</article-id>
<article-id pub-id-type="publisher-id">S0022-2836(08)00940-6</article-id>
<article-id pub-id-type="doi">10.1016/j.jmb.2008.07.071</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
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<title-group><article-title>Variable Oligomerization Modes in Coronavirus Non-structural Protein 9</article-title>
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<email>hilgenfeld@biochem.uni-luebeck.de</email>
<xref rid="aff1" ref-type="aff">1</xref>
<xref rid="aff3" ref-type="aff">3</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>1</label>
Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany</aff>
<aff id="aff2"><label>2</label>
Institute of Chemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany</aff>
<aff id="aff3"><label>3</label>
Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Building 22a, Notkestr. 85, 22603 Hamburg, 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, 23538 Lübeck, Germany. <email>hilgenfeld@biochem.uni-luebeck.de</email>
</corresp>
</author-notes>
<pub-date pub-type="pmc-release"><day>30</day>
<month>7</month>
<year>2008</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"><day>28</day>
<month>11</month>
<year>2008</year>
</pub-date>
<pub-date pub-type="epub"><day>30</day>
<month>7</month>
<year>2008</year>
</pub-date>
<volume>383</volume>
<issue>5</issue>
<fpage>1081</fpage>
<lpage>1096</lpage>
<history><date date-type="received"><day>13</day>
<month>4</month>
<year>2008</year>
</date>
<date date-type="rev-recd"><day>17</day>
<month>7</month>
<year>2008</year>
</date>
<date date-type="accepted"><day>24</day>
<month>7</month>
<year>2008</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2008 Elsevier Ltd. All rights reserved.</copyright-statement>
<copyright-year>2008</copyright-year>
<copyright-holder>Elsevier Ltd</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><p>Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.</p>
</abstract>
<kwd-group><title>Abbreviations</title>
<kwd>SARS-CoV, severe acute respiratory syndrome coronavirus</kwd>
<kwd>HCoV-229E, human coronavirus 229E</kwd>
<kwd>Nsp, non-structural protein</kwd>
<kwd>MPD, 2-methyl-2,4-pentanediol</kwd>
<kwd>DLS, dynamic light-scattering</kwd>
<kwd>M<sup>pro</sup>
, main proteinase</kwd>
<kwd>r.m.s., root-mean-square</kwd>
<kwd>SSB, single-stranded DNA-binding protein</kwd>
<kwd>SPR, surface plasmon resonance</kwd>
<kwd>ssDNA, single-stranded DNA</kwd>
<kwd>ssRNA, single-stranded RNA</kwd>
<kwd>OB, oligonucleotide/oligosaccharide-binding</kwd>
<kwd>pp1a, polyprotein 1a</kwd>
<kwd>RU, resonance units</kwd>
</kwd-group>
<kwd-group><title>Keywords</title>
<kwd>Nsp9</kwd>
<kwd>dimerization</kwd>
<kwd>nucleic-acid binding</kwd>
<kwd>disulfide bond</kwd>
<kwd>oxidative stress</kwd>
</kwd-group>
</article-meta>
<notes><p>Edited by R. Huber</p>
</notes>
</front>
</pmc>
<affiliations><list><country><li>Allemagne</li>
</country>
<region><li>Hambourg</li>
</region>
<settlement><li>Hambourg</li>
</settlement>
</list>
<tree><country name="Allemagne"><noRegion><name sortKey="Ponnusamy, Rajesh" sort="Ponnusamy, Rajesh" uniqKey="Ponnusamy R" first="Rajesh" last="Ponnusamy">Rajesh Ponnusamy</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="Mesters, Jeroen R" sort="Mesters, Jeroen R" uniqKey="Mesters J" first="Jeroen R." last="Mesters">Jeroen R. Mesters</name>
<name sortKey="Moll, Ralf" sort="Moll, Ralf" uniqKey="Moll R" first="Ralf" last="Moll">Ralf Moll</name>
<name sortKey="Weimar, Thomas" sort="Weimar, Thomas" uniqKey="Weimar T" first="Thomas" last="Weimar">Thomas Weimar</name>
</country>
</tree>
</affiliations>
</record>
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