Characterization of mimotopes mimicking an immunodominant conformational epitope on the hepatitis C virus NS3 helicase
Identifieur interne : 000223 ( France/Analysis ); précédent : 000222; suivant : 000224Characterization of mimotopes mimicking an immunodominant conformational epitope on the hepatitis C virus NS3 helicase
Auteurs : Colette Jolivet-Reynaud [France] ; Anne Adida [France] ; Sandrine Michel [France] ; Gilbert Deléage [France] ; Glaucia Paranhos-Baccala [France] ; Virginie Gonin [France] ; Nicole Battail-Poirot [France] ; Xavier Lacoux [France] ; Dominique Rolland [France]Source :
- Journal of Medical Virology [ 0146-6615 ] ; 2004-03.
English descriptors
- Teeft :
- Amino, Amino acid similarities, Amino acids, Antibody, Antigenic, Clone, Cortese, Different mabs, Dodecapeptide library, Elisa, Elisa plate reader, Epitope, Goat serum, Healthy individuals, Helicase, Helicase domain, Helicase mimotopes, Hepatitis, Horizontal line, Human sera, Hydrogen peroxide, Immunodominant, Immunol, Immunoreactivity, Jackson immunoresearch laboratories, Ligand, Mabs, Mimotopes, Molecular modeling, Monaci, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Nahco3 buffer, Nitrocellulose membrane, Ortho phenylene diamine, Peptide, Peptide libraries, Phage, Phage clones, Positive sera, Proc natl acad, Recombinant, Recombinant protein, Recombinant proteins, Seroconversion, Serum, Serum antibodies, Solid phase, Supernatant phages, Synthetic peptides, Virol.
Abstract
The hepatitis C virus (HCV) nonstructural 3 (NS3) protein is composed of an amino terminal protease and a carboxyl terminal RNA helicase. NS3 contains major antigenic epitopes. The antibody response to NS3 appears early in the course of infection and is focused on the helicase region. However, this response cannot be defined by short synthetic peptides indicating the recognition of conformation‐dependent epitopes. In this study, we have screened a dodecapeptide library displayed on phage with anti‐NS3 mouse monoclonal antibodies (mAbs) that compete with each other and human anti‐HCV NS3 positive sera. Two peptides (mimotopes) were selected that appeared to mimic an immunodominant epitope since they were recognized specifically by the different anti‐NS3 mAbs of the study and by human sera from HCV infected patients. Homology search between the two mimotopes and the NS3 sequence showed that one of the two peptides shared amino acid similarities with NS3 at residues 1396–1398 on a very accessible loop as visualized on the three‐dimensional structure of the helicase domain whereas the other one had two amino acids similar to nearby residues 1376 and 1378. Reproduced as synthetic dodecapeptides, the two mimotopes were recognized specifically by 19 and 22, respectively, out of 49 sera from HCV infected patients. These mimotopes allowed also the detection of anti‐NS3 antibodies in sera of HCV patients at the seroconversion stage. These results suggest that the two NS3 mimotopes are potential tools for the diagnosis of HCV infection. J. Med. Virol. 72:385–395, 2004. © 2004 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jmv.20002
Affiliations:
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xml:lang="fr">France</country><wicri:regionArea>Département R&D unité Immunoessais, bioMérieux, Marcy L'etoile</wicri:regionArea><wicri:noRegion>Marcy L'etoile</wicri:noRegion><wicri:noRegion>Marcy L'etoile</wicri:noRegion></affiliation></author><author><name sortKey="Rolland, Dominique" sort="Rolland, Dominique" uniqKey="Rolland D" first="Dominique" last="Rolland">Dominique Rolland</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Département R&D unité Immunoessais, bioMérieux, Marcy L'etoile</wicri:regionArea><wicri:noRegion>Marcy L'etoile</wicri:noRegion><wicri:noRegion>Marcy L'etoile</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Medical Virology</title><title level="j" type="alt">JOURNAL OF MEDICAL VIROLOGY</title><idno type="ISSN">0146-6615</idno><idno type="eISSN">1096-9071</idno><imprint><biblScope unit="vol">72</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="385">385</biblScope><biblScope unit="page" to="395">395</biblScope><biblScope unit="page-count">11</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2004-03">2004-03</date></imprint><idno type="ISSN">0146-6615</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0146-6615</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acid similarities</term><term>Amino acids</term><term>Antibody</term><term>Antigenic</term><term>Clone</term><term>Cortese</term><term>Different mabs</term><term>Dodecapeptide library</term><term>Elisa</term><term>Elisa plate reader</term><term>Epitope</term><term>Goat serum</term><term>Healthy individuals</term><term>Helicase</term><term>Helicase domain</term><term>Helicase mimotopes</term><term>Hepatitis</term><term>Horizontal line</term><term>Human sera</term><term>Hydrogen peroxide</term><term>Immunodominant</term><term>Immunol</term><term>Immunoreactivity</term><term>Jackson immunoresearch laboratories</term><term>Ligand</term><term>Mabs</term><term>Mimotopes</term><term>Molecular modeling</term><term>Monaci</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Nahco3 buffer</term><term>Nitrocellulose membrane</term><term>Ortho phenylene diamine</term><term>Peptide</term><term>Peptide libraries</term><term>Phage</term><term>Phage clones</term><term>Positive sera</term><term>Proc natl acad</term><term>Recombinant</term><term>Recombinant protein</term><term>Recombinant proteins</term><term>Seroconversion</term><term>Serum</term><term>Serum antibodies</term><term>Solid phase</term><term>Supernatant phages</term><term>Synthetic peptides</term><term>Virol</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The hepatitis C virus (HCV) nonstructural 3 (NS3) protein is composed of an amino terminal protease and a carboxyl terminal RNA helicase. NS3 contains major antigenic epitopes. The antibody response to NS3 appears early in the course of infection and is focused on the helicase region. However, this response cannot be defined by short synthetic peptides indicating the recognition of conformation‐dependent epitopes. In this study, we have screened a dodecapeptide library displayed on phage with anti‐NS3 mouse monoclonal antibodies (mAbs) that compete with each other and human anti‐HCV NS3 positive sera. Two peptides (mimotopes) were selected that appeared to mimic an immunodominant epitope since they were recognized specifically by the different anti‐NS3 mAbs of the study and by human sera from HCV infected patients. Homology search between the two mimotopes and the NS3 sequence showed that one of the two peptides shared amino acid similarities with NS3 at residues 1396–1398 on a very accessible loop as visualized on the three‐dimensional structure of the helicase domain whereas the other one had two amino acids similar to nearby residues 1376 and 1378. Reproduced as synthetic dodecapeptides, the two mimotopes were recognized specifically by 19 and 22, respectively, out of 49 sera from HCV infected patients. These mimotopes allowed also the detection of anti‐NS3 antibodies in sera of HCV patients at the seroconversion stage. These results suggest that the two NS3 mimotopes are potential tools for the diagnosis of HCV infection. J. Med. Virol. 72:385–395, 2004. © 2004 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Lyon</li></settlement></list><tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Jolivet Eynaud, Colette" sort="Jolivet Eynaud, Colette" uniqKey="Jolivet Eynaud C" first="Colette" last="Jolivet-Reynaud">Colette Jolivet-Reynaud</name></region><name sortKey="Adida, Anne" sort="Adida, Anne" uniqKey="Adida A" first="Anne" last="Adida">Anne Adida</name><name sortKey="Battail Oirot, Nicole" sort="Battail Oirot, Nicole" uniqKey="Battail Oirot N" first="Nicole" last="Battail-Poirot">Nicole Battail-Poirot</name><name sortKey="Deleage, Gilbert" sort="Deleage, Gilbert" uniqKey="Deleage G" first="Gilbert" last="Deléage">Gilbert Deléage</name><name sortKey="Gonin, Virginie" sort="Gonin, Virginie" uniqKey="Gonin V" first="Virginie" last="Gonin">Virginie Gonin</name><name sortKey="Jolivet Eynaud, Colette" sort="Jolivet Eynaud, Colette" uniqKey="Jolivet Eynaud C" first="Colette" last="Jolivet-Reynaud">Colette Jolivet-Reynaud</name><name sortKey="Jolivet Eynaud, Colette" sort="Jolivet Eynaud, Colette" uniqKey="Jolivet Eynaud C" first="Colette" last="Jolivet-Reynaud">Colette Jolivet-Reynaud</name><name sortKey="Lacoux, Xavier" sort="Lacoux, Xavier" uniqKey="Lacoux X" first="Xavier" last="Lacoux">Xavier Lacoux</name><name sortKey="Michel, Sandrine" sort="Michel, Sandrine" uniqKey="Michel S" first="Sandrine" last="Michel">Sandrine Michel</name><name sortKey="Paranhos Accala, Glaucia" sort="Paranhos Accala, Glaucia" uniqKey="Paranhos Accala G" first="Glaucia" last="Paranhos-Baccala">Glaucia Paranhos-Baccala</name><name sortKey="Rolland, Dominique" sort="Rolland, Dominique" uniqKey="Rolland D" first="Dominique" last="Rolland">Dominique Rolland</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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