SrasV1, Hal, Corpus, bibRecord, 000146

Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains

Identifieur interne : 000146 ( Hal/Corpus ); précédent : 000145; suivant : 000147

Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains

Auteurs : Marie-Pierre Egloff ; Hélène Malet ; Ákos Putics ; Maarit Heinonen ; Hélène Dutartre ; Antoine Frangeul ; Arnaud Gruez ; Valérie Campanacci ; Christian Cambillau ; John Ziebuhr ; Tero Ahola ; Bruno Canard

Source :

Journal of Virology [ 0022-538X ] ; 2006-08-15.

RBID : Hal:hal-02459228

Abstract

Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.

Url:

https://hal.archives-ouvertes.fr/hal-02459228

DOI: 10.1128/JVI.00713-06

Links to Exploration step

Hal:hal-02459228

Le document en format XML

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<author><name sortKey="Malet, Helene" sort="Malet, Helene" uniqKey="Malet H" first="Hélène" last="Malet">Hélène Malet</name>
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<author><name sortKey="Putics, Akos" sort="Putics, Akos" uniqKey="Putics A" first="Ákos" last="Putics">Ákos Putics</name>
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<author><name sortKey="Heinonen, Maarit" sort="Heinonen, Maarit" uniqKey="Heinonen M" first="Maarit" last="Heinonen">Maarit Heinonen</name>
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<author><name sortKey="Frangeul, Antoine" sort="Frangeul, Antoine" uniqKey="Frangeul A" first="Antoine" last="Frangeul">Antoine Frangeul</name>
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<author><name sortKey="Gruez, Arnaud" sort="Gruez, Arnaud" uniqKey="Gruez A" first="Arnaud" last="Gruez">Arnaud Gruez</name>
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<author><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name>
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          <orgName>Université de Provence - Aix-Marseille 1</orgName>
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<author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name>
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          <orgName>Architecture et fonction des Macromolécules Biologiques - UMR 6098</orgName>
          <orgName type="acronym">AFMB</orgName>
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          <date type="end">2011</date>
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<author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name>
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          <desc>            <address>              <addrLine>Sanderring 297070 Würzburg </addrLine>
              <country key="DE"></country>
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            <ref type="url">https://www.uni-wuerzburg.de/en/university/</ref>
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<author><name sortKey="Ahola, Tero" sort="Ahola, Tero" uniqKey="Ahola T" first="Tero" last="Ahola">Tero Ahola</name>
<affiliation><hal:affiliation type="institution" xml:id="struct-50895" status="VALID">          <orgName>University of Helsinki</orgName>
          <desc>            <address>              <addrLine>Yliopistonkatu 4, 00100 Helsinki</addrLine>
              <country key="FI"></country>
            </address>
            <ref type="url">https://www.helsinki.fi/en</ref>
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<author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-199349" status="OLD">          <idno type="IdRef">149981651</idno>
          <idno type="RNSR">201220260Z</idno>
          <orgName>Architecture et fonction des macromolécules biologiques</orgName>
          <orgName type="acronym">AFMB</orgName>
          <date type="start">2012-01-01</date>
          <date type="end">2019-12-31</date>
          <desc>            <address>              <addrLine>Faculté des Sciences de Luminy - Case 932 163, Avenue de Luminy13288 Marseille Cedex 09</addrLine>
              <country key="FR"></country>
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          <orgName type="acronym">INRA</orgName>
          <date type="start">1946-05-18</date>
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          <orgName>Aix Marseille Université</orgName>
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          <date type="start">2012-01-01</date>
          <desc>            <address>              <addrLine>Aix-Marseille UniversitéJardins du Pharo58 Boulevard Charles Livon13284 Marseille cedex 7</addrLine>
              <country key="FR"></country>
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          <orgName>Centre National de la Recherche Scientifique</orgName>
          <orgName type="acronym">CNRS</orgName>
          <date type="start">1939-10-19</date>
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</analytic>
<idno type="DOI">10.1128/JVI.00713-06</idno>
<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date type="datePub">2006-08-15</date>
</imprint>
</series>
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<front><div type="abstract" xml:lang="en">              <p>Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.</p>
            </div>
</front>
</TEI>
<hal api="V3">          <titleStmt>            <title xml:lang="en">Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains</title>
            <author role="aut">              <persName>                <forename type="first">Marie-Pierre</forename>
                <surname>Egloff</surname>
              </persName>
              <idno type="halauthorid">11434122</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Hélène</forename>
                <surname>Malet</surname>
              </persName>
              <idno type="halauthorid">1112974</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Ákos</forename>
                <surname>Putics</surname>
              </persName>
              <idno type="halauthorid">507160</idno>
              <affiliation ref="#struct-306583"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Maarit</forename>
                <surname>Heinonen</surname>
              </persName>
              <idno type="halauthorid">1213225</idno>
              <affiliation ref="#struct-50895"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Hélène</forename>
                <surname>Dutartre</surname>
              </persName>
              <idno type="halauthorid">434484</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Antoine</forename>
                <surname>Frangeul</surname>
              </persName>
              <idno type="halauthorid">11430256</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Arnaud</forename>
                <surname>Gruez</surname>
              </persName>
              <idno type="halauthorid">1473095</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Valérie</forename>
                <surname>Campanacci</surname>
              </persName>
              <idno type="halauthorid">234470</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Christian</forename>
                <surname>Cambillau</surname>
              </persName>
              <idno type="halauthorid">234469</idno>
              <affiliation ref="#struct-482300"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">John</forename>
                <surname>Ziebuhr</surname>
              </persName>
              <idno type="halauthorid">11740211</idno>
              <affiliation ref="#struct-306583"></affiliation>
              <affiliation ref="#struct-458815"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Tero</forename>
                <surname>Ahola</surname>
              </persName>
              <idno type="halauthorid">11734886</idno>
              <affiliation ref="#struct-50895"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Bruno</forename>
                <surname>Canard</surname>
              </persName>
              <email type="md5">b082b648c100da933978ce65df2a1ad4</email>
              <email type="domain">afmb.univ-mrs.fr</email>
              <idno type="halauthorid">728889</idno>
              <affiliation ref="#struct-199349"></affiliation>
            </author>
            <editor role="depositor">              <persName>                <forename>Helene</forename>
                <surname>Dutartre</surname>
              </persName>
              <email type="md5">e9950f5e032f5510dd65c5ed2f354324</email>
              <email type="domain">ens-lyon.fr</email>
            </editor>
          </titleStmt>
          <editionStmt>            <edition n="v1" type="current">              <date type="whenSubmitted">2020-01-29 11:44:10</date>
              <date type="whenModified">2020-03-17 03:38:44</date>
              <date type="whenReleased">2020-01-29 11:44:10</date>
              <date type="whenProduced">2006-08-15</date>
              <ref type="externalLink" target="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1563857/pdf"></ref>
            </edition>
            <respStmt>              <resp>contributor</resp>
              <name key="41154">                <persName>                  <forename>Helene</forename>
                  <surname>Dutartre</surname>
                </persName>
                <email type="md5">e9950f5e032f5510dd65c5ed2f354324</email>
                <email type="domain">ens-lyon.fr</email>
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            <idno type="halBibtex">egloff:hal-02459228</idno>
            <idno type="halRefHtml">Journal of Virology, American Society for Microbiology, 2006, 80 (17), pp.8493-8502. ⟨10.1128/JVI.00713-06⟩</idno>
            <idno type="halRef">Journal of Virology, American Society for Microbiology, 2006, 80 (17), pp.8493-8502. ⟨10.1128/JVI.00713-06⟩</idno>
          </publicationStmt>
          <seriesStmt>            <idno type="stamp" n="UGA">HAL Grenoble Alpes</idno>
            <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
            <idno type="stamp" n="UNIV-GRENOBLE1" corresp="UGA">Université Joseph Fourier - Grenoble I</idno>
            <idno type="stamp" n="IBS" corresp="CEA">Institut de Biologie Structurale</idno>
            <idno type="stamp" n="CEA">CEA - Commissariat à l'énergie atomique</idno>
            <idno type="stamp" n="IBS-MEM" corresp="IBS">Groupe Microscopie Electronique et Méthodes / Methods and Electron Microscopy Group (IBS-MEM)</idno>
            <idno type="stamp" n="INRA">INRA - Institut national de la recherche agronomique</idno>
            <idno type="stamp" n="UNIV-AMU">Aix Marseille Université</idno>
            <idno type="stamp" n="TEST-AMU">Espace de test AMU</idno>
            <idno type="stamp" n="INRAE">Institut National de Recherche en Agriculture, Alimentation et Environnement</idno>
          </seriesStmt>
          <notesStmt>            <note type="audience" n="2">International</note>
            <note type="popular" n="0">No</note>
            <note type="peer" n="1">Yes</note>
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          <sourceDesc>            <biblStruct>              <analytic>                <title xml:lang="en">Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains</title>
                <author role="aut">                  <persName>                    <forename type="first">Marie-Pierre</forename>
                    <surname>Egloff</surname>
                  </persName>
                  <idno type="halauthorid">11434122</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Hélène</forename>
                    <surname>Malet</surname>
                  </persName>
                  <idno type="halauthorid">1112974</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Ákos</forename>
                    <surname>Putics</surname>
                  </persName>
                  <idno type="halauthorid">507160</idno>
                  <affiliation ref="#struct-306583"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Maarit</forename>
                    <surname>Heinonen</surname>
                  </persName>
                  <idno type="halauthorid">1213225</idno>
                  <affiliation ref="#struct-50895"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Hélène</forename>
                    <surname>Dutartre</surname>
                  </persName>
                  <idno type="halauthorid">434484</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Antoine</forename>
                    <surname>Frangeul</surname>
                  </persName>
                  <idno type="halauthorid">11430256</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Arnaud</forename>
                    <surname>Gruez</surname>
                  </persName>
                  <idno type="halauthorid">1473095</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Valérie</forename>
                    <surname>Campanacci</surname>
                  </persName>
                  <idno type="halauthorid">234470</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Christian</forename>
                    <surname>Cambillau</surname>
                  </persName>
                  <idno type="halauthorid">234469</idno>
                  <affiliation ref="#struct-482300"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">John</forename>
                    <surname>Ziebuhr</surname>
                  </persName>
                  <idno type="halauthorid">11740211</idno>
                  <affiliation ref="#struct-306583"></affiliation>
                  <affiliation ref="#struct-458815"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Tero</forename>
                    <surname>Ahola</surname>
                  </persName>
                  <idno type="halauthorid">11734886</idno>
                  <affiliation ref="#struct-50895"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Bruno</forename>
                    <surname>Canard</surname>
                  </persName>
                  <email type="md5">b082b648c100da933978ce65df2a1ad4</email>
                  <email type="domain">afmb.univ-mrs.fr</email>
                  <idno type="halauthorid">728889</idno>
                  <affiliation ref="#struct-199349"></affiliation>
                </author>
              </analytic>
              <monogr>                <idno type="halJournalId" status="VALID">6614</idno>
                <idno type="issn">0022-538X</idno>
                <idno type="eissn">1098-5514</idno>
                <title level="j">Journal of Virology</title>
                <imprint>                  <publisher>American Society for Microbiology</publisher>
                  <biblScope unit="volume">80</biblScope>
                  <biblScope unit="issue">17</biblScope>
                  <biblScope unit="pp">8493-8502</biblScope>
                  <date type="datePub">2006-08-15</date>
                </imprint>
              </monogr>
              <idno type="doi">10.1128/JVI.00713-06</idno>
              <idno type="pubmed">16912299</idno>
              <idno type="pubmedcentral">PMC1563857</idno>
            </biblStruct>
          </sourceDesc>
          <profileDesc>            <langUsage>              <language ident="en">English</language>
            </langUsage>
            <textClass>              <classCode scheme="halDomain" n="sdv.mp.vir">Life Sciences [q-bio]/Microbiology and Parasitology/Virology</classCode>
              <classCode scheme="halDomain" n="sdv.bbm.bs">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
            </textClass>
            <abstract xml:lang="en">              <p>Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.</p>
            </abstract>
          </profileDesc>
        </hal>
</record>

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Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains

Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains

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