MersV1, France, Analysis, bibRecord, 000176

Inhibition of vaccinia virus replication by peptide aptamers

Identifieur interne : 000176 ( France/Analysis ); précédent : 000175; suivant : 000177

Inhibition of vaccinia virus replication by peptide aptamers

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

Source :

Antiviral research [ 0166-3542 ] ; 2009.

RBID : Pascal:09-0230827

Descripteurs français

KwdFr :
- ADN viral (biosynthèse), Antiviraux (pharmacologie), Aptamères peptidiques (pharmacologie), Cartographie d'interactions entre protéines, Humains, Liaison aux protéines, Lignée cellulaire, Protéines virales (métabolisme), Réplication virale (), Techniques de double hybride, Virus de la vaccine (), Virus de la vaccine (physiologie).
MESH :
- biosynthèse : ADN viral.
- métabolisme : Protéines virales.
- pharmacologie : Antiviraux, Aptamères peptidiques.
- physiologie : Virus de la vaccine.
Pascal (Inist)
- Cartographie d'interactions entre protéines, Humains, Inhibition, Liaison aux protéines, Lignée cellulaire, Réplication virale, Techniques de double hybride, Virus de la vaccine, Virus vaccine, Réplication, Peptide, Aptamère, Levure, Génétique, Antiviral, In vitro.
Wicri :
- topic : Génétique.

English descriptors

KwdEn :
- Antiviral, Antiviral Agents (pharmacology), Aptamer, Aptamers, Peptide (pharmacology), Cell Line, DNA, Viral (biosynthesis), Genetics, Humans, In vitro, Inhibition, Peptides, Protein Binding, Protein Interaction Mapping, Replication, Two-Hybrid System Techniques, Vaccinia virus, Vaccinia virus (drug effects), Vaccinia virus (physiology), Viral Proteins (metabolism), Virus Replication (drug effects), Yeast.
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.

Url:

https://hal.archives-ouvertes.fr/hal-00416045

Affiliations:

Links to Exploration step

Pascal:09-0230827

Le document en format XML

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<term>DNA, Viral (biosynthesis)</term>
<term>Genetics</term>
<term>Humans</term>
<term>In vitro</term>
<term>Inhibition</term>
<term>Peptides</term>
<term>Protein Binding</term>
<term>Protein Interaction Mapping</term>
<term>Replication</term>
<term>Two-Hybrid System Techniques</term>
<term>Vaccinia virus</term>
<term>Vaccinia virus (drug effects)</term>
<term>Vaccinia virus (physiology)</term>
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<term>Cartographie d'interactions entre protéines</term>
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<term>Protéines virales (métabolisme)</term>
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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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<tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Saccucci, Laurent" sort="Saccucci, Laurent" uniqKey="Saccucci L" first="Laurent" last="Saccucci">Laurent Saccucci</name>
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<name sortKey="Crance, Jean Marc" sort="Crance, Jean Marc" uniqKey="Crance J" first="Jean-Marc" last="Crance">Jean-Marc Crance</name>
<name sortKey="Garin, Daniel" sort="Garin, Daniel" uniqKey="Garin D" first="Daniel" last="Garin">Daniel Garin</name>
<name sortKey="Iseni, Frederic" sort="Iseni, Frederic" uniqKey="Iseni F" first="Frédéric" last="Iseni">Frédéric Iseni</name>
<name sortKey="Saccucci, Laurent" sort="Saccucci, Laurent" uniqKey="Saccucci L" first="Laurent" last="Saccucci">Laurent Saccucci</name>
</country>
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Serveur d'exploration MERS

Inhibition of vaccinia virus replication by peptide aptamers

Inhibition of vaccinia virus replication by peptide aptamers

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

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	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.