MersV1, PascalFrancis, Checkpoint, bibRecord, 000066

Inhibition of vaccinia virus replication by peptide aptamers

Identifieur interne : 000066 ( PascalFrancis/Checkpoint ); précédent : 000065; suivant : 000067

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

Pascal (Inist)
- Inhibition, Virus vaccine, Réplication, Peptide, Aptamère, Levure, Génétique, Antiviral, In vitro.
Wicri :
- topic : Génétique.

English descriptors

KwdEn :
- Antiviral, Aptamer, Genetics, In vitro, Inhibition, Peptides, Replication, Vaccinia virus, Yeast.

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.

Affiliations:

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Le document en format XML

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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>
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<fC07 i1="01" i2="X" l="FRE"><s0>Orthopoxvirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Orthopoxvirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Orthopoxvirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Chordopoxvirinae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Chordopoxvirinae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Chordopoxvirinae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Poxviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Poxviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Poxviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fN21><s1>166</s1>
</fN21>
</pA>
</standard>
</inist>
<affiliations><list><country><li>France</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
</region>
<settlement><li>Grenoble</li>
<li>Lyon</li>
</settlement>
</list>
<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>
</region>
<name sortKey="Bickle, Marc" sort="Bickle, Marc" uniqKey="Bickle M" first="Marc" last="Bickle">Marc Bickle</name>
<name sortKey="Colas, Pierre" sort="Colas, Pierre" uniqKey="Colas P" first="Pierre" last="Colas">Pierre Colas</name>
<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>
</tree>
</affiliations>
</record>

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   |texte=   Inhibition of vaccinia virus replication by peptide aptamers
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Inhibition of vaccinia virus replication by peptide aptamers

Inhibition of vaccinia virus replication by peptide aptamers

Source :

Descripteurs français

English descriptors

Abstract

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