MersV1, PubMed, Corpus, bibRecord, 002015

Inhibition of vaccinia virus replication by peptide aptamers.

Identifieur interne : 002015 ( PubMed/Corpus ); précédent : 002014; suivant : 002016

Inhibition of vaccinia virus replication by peptide aptamers.

Auteurs : Laurent Saccucci ; Jean-Marc Crance ; Pierre Colas ; Marc Bickle ; Daniel Garin ; Frédéric Iseni

Source :

Antiviral research [ 1872-9096 ] ; 2009.

RBID : pubmed:19428604

English descriptors

KwdEn :
- Antiviral Agents (pharmacology), Aptamers, Peptide (pharmacology), Cell Line, DNA, Viral (biosynthesis), Humans, Protein Binding, Protein Interaction Mapping, Two-Hybrid System Techniques, Vaccinia virus (drug effects), Vaccinia virus (physiology), Viral Proteins (metabolism), Virus Replication (drug effects).
MESH :
- chemical , biosynthesis : DNA, Viral.
- chemical , metabolism : Viral Proteins.
- chemical , pharmacology : Antiviral Agents, Aptamers, Peptide.
- drug effects : Vaccinia virus, Virus Replication.
- physiology : Vaccinia virus.
- Cell Line, Humans, Protein Binding, Protein Interaction Mapping, Two-Hybrid System Techniques.

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.

DOI: 10.1016/j.antiviral.2009.02.191
PubMed: 19428604

Links to Exploration step

pubmed:19428604

Le document en format XML

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<author><name sortKey="Saccucci, Laurent" sort="Saccucci, Laurent" uniqKey="Saccucci L" first="Laurent" last="Saccucci">Laurent Saccucci</name>
<affiliation><nlm:affiliation>Institut de Recherches Biomédicales des Armées, CRSSA Emile Pardé, Grenoble, France.</nlm:affiliation>
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<author><name sortKey="Crance, Jean Marc" sort="Crance, Jean Marc" uniqKey="Crance J" first="Jean-Marc" last="Crance">Jean-Marc Crance</name>
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<author><name sortKey="Colas, Pierre" sort="Colas, Pierre" uniqKey="Colas P" first="Pierre" last="Colas">Pierre Colas</name>
</author>
<author><name sortKey="Bickle, Marc" sort="Bickle, Marc" uniqKey="Bickle M" first="Marc" last="Bickle">Marc Bickle</name>
</author>
<author><name sortKey="Garin, Daniel" sort="Garin, Daniel" uniqKey="Garin D" first="Daniel" last="Garin">Daniel Garin</name>
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<author><name sortKey="Iseni, Frederic" sort="Iseni, Frederic" uniqKey="Iseni F" first="Frédéric" last="Iseni">Frédéric Iseni</name>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<Abstract><AbstractText>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.</AbstractText>
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Inhibition of vaccinia virus replication by peptide aptamers.

Inhibition of vaccinia virus replication by peptide aptamers.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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