Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication
Identifieur interne : 000572 ( Pmc/Checkpoint ); précédent : 000571; suivant : 000573Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication
Auteurs : Yusuke Sakai [Japon] ; Kengo Kawachi [Japon] ; Yutaka Terada [Japon] ; Hiroko Omori [Japon] ; Yoshiharu Matsuura [Japon] ; Wataru Kamitani [Japon]Source :
- Virology [ 0042-6822 ] ; 2017.
Abstract
Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.
Url:
DOI: 10.1016/j.virol.2017.07.019
PubMed: 28738245
PubMed Central: 7111695
Affiliations:
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PMC:7111695Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.</p>
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<author><name sortKey="Bestebroer, T M" uniqKey="Bestebroer T">T.M. Bestebroer</name>
</author>
<author><name sortKey="Osterhaus, A D" uniqKey="Osterhaus A">A.D. Osterhaus</name>
</author>
<author><name sortKey="Fouchier, R A" uniqKey="Fouchier R">R.A. Fouchier</name>
</author>
</analytic>
</biblStruct>
</listBibl>
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</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Virology</journal-id>
<journal-id journal-id-type="iso-abbrev">Virology</journal-id>
<journal-title-group><journal-title>Virology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0042-6822</issn>
<issn pub-type="epub">1096-0341</issn>
<publisher><publisher-name>Elsevier Inc.</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">28738245</article-id>
<article-id pub-id-type="pmc">7111695</article-id>
<article-id pub-id-type="publisher-id">S0042-6822(17)30238-6</article-id>
<article-id pub-id-type="doi">10.1016/j.virol.2017.07.019</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" id="au0005"><name><surname>Sakai</surname>
<given-names>Yusuke</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
<xref rid="aff0020" ref-type="aff">d</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author" id="au0010"><name><surname>Kawachi</surname>
<given-names>Kengo</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
<xref rid="aff0010" ref-type="aff">b</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author" id="au0015"><name><surname>Terada</surname>
<given-names>Yutaka</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au0020"><name><surname>Omori</surname>
<given-names>Hiroko</given-names>
</name>
<xref rid="aff0015" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author" id="au0025"><name><surname>Matsuura</surname>
<given-names>Yoshiharu</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author" id="au0030"><name><surname>Kamitani</surname>
<given-names>Wataru</given-names>
</name>
<email>wakamita@biken.osaka-u.ac.jp</email>
<xref rid="aff0005" ref-type="aff">a</xref>
<xref rid="aff0025" ref-type="aff">e</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
</contrib-group>
<aff id="aff0005"><label>a</label>
Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan</aff>
<aff id="aff0010"><label>b</label>
Department of Molecular Virology, Osaka, Japan</aff>
<aff id="aff0015"><label>c</label>
Core Instrumentation Facility, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan</aff>
<aff id="aff0020"><label>d</label>
Laboratory of Veterinary Pathology, Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi, Japan</aff>
<aff id="aff0025"><label>e</label>
Tsukuba Primate Research Center, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan</aff>
<author-notes><corresp id="cor1"><label>⁎</label>
Correspondence to: Laboratory of Clinical Research on Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita-shi, Osaka 565-0871, Japan. <email>wakamita@biken.osaka-u.ac.jp</email>
</corresp>
<fn id="fn1"><label>1</label>
<p id="ntp0005">These authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release"><day>21</day>
<month>7</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>10</month>
<year>2017</year>
</pub-date>
<pub-date pub-type="epub"><day>21</day>
<month>7</month>
<year>2017</year>
</pub-date>
<volume>510</volume>
<fpage>165</fpage>
<lpage>174</lpage>
<history><date date-type="received"><day>5</day>
<month>6</month>
<year>2017</year>
</date>
<date date-type="rev-recd"><day>9</day>
<month>7</month>
<year>2017</year>
</date>
<date date-type="accepted"><day>14</day>
<month>7</month>
<year>2017</year>
</date>
</history>
<permissions><copyright-statement>© 2017 Elsevier Inc.</copyright-statement>
<copyright-year>2017</copyright-year>
<copyright-holder>Elsevier Inc.</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="ab0010"><p>Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.</p>
</abstract>
<abstract abstract-type="author-highlights" id="ab0015"><title>Highlights</title>
<p><list list-type="simple" id="li0005"><list-item id="u0005"><label>•</label>
<p id="p0005">H120 and F121 in the lumenal loop in nsp4 are essential for binding to nsp3.</p>
</list-item>
<list-item id="u0010"><label>•</label>
<p id="p0010">H120&F121 substitutions in nsp4 cause defect in membrane rearrangement function.</p>
</list-item>
<list-item id="u0015"><label>•</label>
<p id="p0015">Interaction with nsp3 through H120&F121 in nsp4 is crucial for viral propagation.</p>
</list-item>
</list>
</p>
</abstract>
<kwd-group id="keys0005"><title>Keywords</title>
<kwd>Coronavirus</kwd>
<kwd>Severe acute respiratory syndrome</kwd>
<kwd>Nsp4</kwd>
<kwd>Viral replication</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Japon</li>
</country>
</list>
<tree><country name="Japon"><noRegion><name sortKey="Sakai, Yusuke" sort="Sakai, Yusuke" uniqKey="Sakai Y" first="Yusuke" last="Sakai">Yusuke Sakai</name>
</noRegion>
<name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name>
<name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name>
<name sortKey="Kawachi, Kengo" sort="Kawachi, Kengo" uniqKey="Kawachi K" first="Kengo" last="Kawachi">Kengo Kawachi</name>
<name sortKey="Kawachi, Kengo" sort="Kawachi, Kengo" uniqKey="Kawachi K" first="Kengo" last="Kawachi">Kengo Kawachi</name>
<name sortKey="Matsuura, Yoshiharu" sort="Matsuura, Yoshiharu" uniqKey="Matsuura Y" first="Yoshiharu" last="Matsuura">Yoshiharu Matsuura</name>
<name sortKey="Omori, Hiroko" sort="Omori, Hiroko" uniqKey="Omori H" first="Hiroko" last="Omori">Hiroko Omori</name>
<name sortKey="Sakai, Yusuke" sort="Sakai, Yusuke" uniqKey="Sakai Y" first="Yusuke" last="Sakai">Yusuke Sakai</name>
<name sortKey="Terada, Yutaka" sort="Terada, Yutaka" uniqKey="Terada Y" first="Yutaka" last="Terada">Yutaka Terada</name>
</country>
</tree>
</affiliations>
</record>
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