Inhibition of vaccinia virus replication by peptide aptamers.
Identifieur interne : 000687 ( Ncbi/Curation ); précédent : 000686; suivant : 000688Inhibition of vaccinia virus replication by peptide aptamers.
Auteurs : Laurent Saccucci [France] ; Jean-Marc Crance ; Pierre Colas ; Marc Bickle ; Daniel Garin ; Frédéric IseniSource :
- Antiviral research [ 1872-9096 ] ; 2009.
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.
- Cartographie d'interactions entre protéines, Humains, Liaison aux protéines, Lignée cellulaire, Réplication virale, Techniques de double hybride, Virus de la vaccine.
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
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(physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>DNA, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Aptamers, Peptide</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>ADN viral</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Vaccinia virus</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term><term>Aptamères peptidiques</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus de la vaccine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Vaccinia virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Protein Binding</term><term>Protein Interaction Mapping</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cartographie d'interactions entre protéines</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Réplication virale</term><term>Techniques de double hybride</term><term>Virus de la vaccine</term></keywords></textClass></profileDesc></teiHeader><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></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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