Inhibition of vaccinia virus replication by peptide aptamers.
Identifieur interne : 000024 ( Hal/Checkpoint ); précédent : 000023Inhibition of vaccinia virus replication by peptide aptamers.
Auteurs : Laurent Saccucci ; Jean-Marc Crance [France] ; Pierre Colas [France] ; Marc Bickle [France] ; Daniel Garin [France] ; Frédéric Iseni [France]Source :
- Antiviral Research [ 0166-3542 ] ; 2009-06.
Abstract
A20 protein is a major component of the vaccinia virus replication complex. It binds to the DNA polymerase E9, the uracil DNA glycosylase D4 and the primase/helicase D5, three proteins that are essential for viral DNA synthesis. The identification of molecules able to interact with the replication complex and inhibit its activity is a promising strategy for the design of new anti-orthopoxvirus drugs. In this study, we used a yeast genetic approach to select, from combinatorial libraries, 8-mers peptide aptamers that specifically interact with A20. From this screen, we isolated five peptide aptamers whose binding to A20 was confirmed by a glutathione S-transferase (GST) pull-down assay. Among those, we determined that peptide aptamer 72 binds to a central domain on A20. Interestingly, this region of A20 was previously shown to be important for its function in DNA replication. We next showed that vaccinia virus DNA synthesis was impaired in cells constitutively expressing peptide aptamer 72 and that virus production was inhibited in those cells. Thus, peptide aptamer 72 may be a useful tool for the development of new compounds specifically targeting poxvirus replication.
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DOI: 10.1016/j.antiviral.2009.02.191
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It binds to the DNA polymerase E9, the uracil DNA glycosylase D4 and the primase/helicase D5, three proteins that are essential for viral DNA synthesis. The identification of molecules able to interact with the replication complex and inhibit its activity is a promising strategy for the design of new anti-orthopoxvirus drugs. In this study, we used a yeast genetic approach to select, from combinatorial libraries, 8-mers peptide aptamers that specifically interact with A20. From this screen, we isolated five peptide aptamers whose binding to A20 was confirmed by a glutathione S-transferase (GST) pull-down assay. Among those, we determined that peptide aptamer 72 binds to a central domain on A20. Interestingly, this region of A20 was previously shown to be important for its function in DNA replication. We next showed that vaccinia virus DNA synthesis was impaired in cells constitutively expressing peptide aptamer 72 and that virus production was inhibited in those cells. Thus, peptide aptamer 72 may be a useful tool for the development of new compounds specifically targeting poxvirus replication.</p> </div></front></TEI><hal api="V3"> <titleStmt> <title xml:lang="en">Inhibition of vaccinia virus replication by peptide aptamers.</title> <author role="aut"> <persName> <forename type="first">Laurent</forename> <surname>Saccucci</surname> </persName> <idno type="halauthorid">431908</idno> </author> <author role="aut"> <persName> <forename type="first">Jean-Marc</forename> <surname>Crance</surname> </persName> <idno type="halauthorid">228230</idno> <affiliation ref="#struct-92699"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Pierre</forename> <surname>Colas</surname> </persName> <idno type="halauthorid">429664</idno> <affiliation ref="#struct-53946"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Marc</forename> <surname>Bickle</surname> </persName> <idno type="halauthorid">343856</idno> <affiliation ref="#struct-71042"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Daniel</forename> <surname>Garin</surname> </persName> <idno type="halauthorid">228231</idno> <affiliation ref="#struct-50663"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Frédéric</forename> <surname>Iseni</surname> </persName> <idno type="halauthorid">431909</idno> <affiliation ref="#struct-714"></affiliation> </author> <editor role="depositor"> <persName> <forename>Allison</forename> <surname>Favey</surname> </persName> <email type="md5">cd2ca3aff86b73ecb2097e2a5444bda7</email> <email type="domain">sb-roscoff.fr</email> </editor> </titleStmt> <editionStmt> <edition n="v1" type="current"> <date type="whenSubmitted">2009-09-11 17:01:33</date> <date type="whenModified">2020-02-10 18:12:58</date> <date type="whenReleased">2009-09-11 17:01:33</date> <date type="whenProduced">2009-06</date> </edition> <respStmt> <resp>contributor</resp> <name key="143528"> <persName> <forename>Allison</forename> <surname>Favey</surname> </persName> <email type="md5">cd2ca3aff86b73ecb2097e2a5444bda7</email> <email type="domain">sb-roscoff.fr</email> </name> </respStmt> </editionStmt> <publicationStmt> <distributor>CCSD</distributor> <idno type="halId">hal-00416045</idno> <idno type="halUri">https://hal.archives-ouvertes.fr/hal-00416045</idno> <idno type="halBibtex">saccucci:hal-00416045</idno> <idno type="halRefHtml">Antiviral Research, Elsevier Masson, 2009, 82 (3), pp.134-40. ⟨10.1016/j.antiviral.2009.02.191⟩</idno> <idno type="halRef">Antiviral Research, Elsevier Masson, 2009, 82 (3), pp.134-40. ⟨10.1016/j.antiviral.2009.02.191⟩</idno> </publicationStmt> <seriesStmt> <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno> <idno type="stamp" n="CEA">CEA - Commissariat à l'énergie atomique</idno> <idno type="stamp" n="DSM-IRFU" corresp="CEA">IRFU</idno> <idno type="stamp" n="SSA">Service de Santé des Armées</idno> <idno type="stamp" n="UNIV-LYON1">Université Claude Bernard - Lyon I</idno> <idno type="stamp" n="CEA-DRF" corresp="CEA">Direction de Recherche Fondamentale</idno> <idno type="stamp" n="MONTPELLIER-SUPAGRO">MONTPELLIER-SUPAGRO</idno> <idno type="stamp" n="UDL">UDL</idno> <idno type="stamp" n="UNIV-LYON">Université de Lyon</idno> </seriesStmt> <notesStmt> <note type="audience" n="2">International</note> <note type="popular" n="0">No</note> <note type="peer" n="1">Yes</note> </notesStmt> <sourceDesc> <biblStruct> <analytic> <title xml:lang="en">Inhibition of vaccinia virus replication by peptide aptamers.</title> <author role="aut"> <persName> <forename type="first">Laurent</forename> <surname>Saccucci</surname> </persName> <idno type="halauthorid">431908</idno> </author> <author role="aut"> <persName> <forename type="first">Jean-Marc</forename> <surname>Crance</surname> </persName> <idno type="halauthorid">228230</idno> <affiliation ref="#struct-92699"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Pierre</forename> <surname>Colas</surname> </persName> <idno type="halauthorid">429664</idno> <affiliation ref="#struct-53946"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Marc</forename> <surname>Bickle</surname> </persName> <idno type="halauthorid">343856</idno> <affiliation ref="#struct-71042"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Daniel</forename> <surname>Garin</surname> </persName> <idno type="halauthorid">228231</idno> <affiliation ref="#struct-50663"></affiliation> </author> <author role="aut"> <persName> <forename type="first">Frédéric</forename> <surname>Iseni</surname> </persName> <idno type="halauthorid">431909</idno> <affiliation ref="#struct-714"></affiliation> </author> </analytic> <monogr> <idno type="halJournalId" status="VALID">10572</idno> <idno type="issn">0166-3542</idno> <title level="j">Antiviral Research</title> <imprint> <publisher>Elsevier Masson</publisher> <biblScope unit="volume">82</biblScope> <biblScope unit="issue">3</biblScope> <biblScope unit="pp">134-40</biblScope> <date type="datePub">2009-06</date> <date type="dateEpub">2009-02-27</date> </imprint> </monogr> <idno type="doi">10.1016/j.antiviral.2009.02.191</idno> <idno type="pubmed">19428604</idno> </biblStruct> </sourceDesc> <profileDesc> <langUsage> <language ident="en">English</language> </langUsage> <textClass> <classCode scheme="mesh">Antiviral Agents</classCode> <classCode scheme="mesh">Aptamers, Peptide</classCode> <classCode scheme="mesh">Virus Replication</classCode> <classCode scheme="mesh">Cell Line</classCode> <classCode scheme="mesh">DNA, Viral</classCode> <classCode scheme="mesh">Humans</classCode> <classCode scheme="mesh">Protein Binding</classCode> <classCode scheme="mesh">Protein Interaction Mapping</classCode> <classCode scheme="mesh">Two-Hybrid System Techniques</classCode> <classCode scheme="mesh">Vaccinia virus</classCode> <classCode scheme="mesh">Viral Proteins</classCode> <classCode scheme="halDomain" n="sdv.bc">Life Sciences [q-bio]/Cellular Biology</classCode> <classCode scheme="halTypology" n="ART">Journal articles</classCode> </textClass> <abstract xml:lang="en"> <p>A20 protein is a major component of the vaccinia virus replication complex. It binds to the DNA polymerase E9, the uracil DNA glycosylase D4 and the primase/helicase D5, three proteins that are essential for viral DNA synthesis. The identification of molecules able to interact with the replication complex and inhibit its activity is a promising strategy for the design of new anti-orthopoxvirus drugs. In this study, we used a yeast genetic approach to select, from combinatorial libraries, 8-mers peptide aptamers that specifically interact with A20. From this screen, we isolated five peptide aptamers whose binding to A20 was confirmed by a glutathione S-transferase (GST) pull-down assay. Among those, we determined that peptide aptamer 72 binds to a central domain on A20. Interestingly, this region of A20 was previously shown to be important for its function in DNA replication. We next showed that vaccinia virus DNA synthesis was impaired in cells constitutively expressing peptide aptamer 72 and that virus production was inhibited in those cells. Thus, peptide aptamer 72 may be a useful tool for the development of new compounds specifically targeting poxvirus replication.</p> </abstract> </profileDesc> </hal></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Sante
|area= MersV1
|flux= Hal
|étape= Checkpoint
|type= RBID
|clé= Hal:hal-00416045
|texte= Inhibition of vaccinia virus replication by peptide aptamers.
}}
| This area was generated with Dilib version V0.6.33. |  |