Identification of an immunodominant B cell epitope on the hepatitis C virus nonstructural region defined by human monoclonal antibodies.
Identifieur interne : 004878 ( Main/Exploration ); précédent : 004877; suivant : 004879Identification of an immunodominant B cell epitope on the hepatitis C virus nonstructural region defined by human monoclonal antibodies.
Auteurs : A. Cerino [Italie] ; M U MondelliSource :
- Journal of immunology (Baltimore, Md. : 1950) [ 0022-1767 ] ; 1991.
Descripteurs français
- KwdFr :
- Anticorps monoclonaux (immunologie), Capside (immunologie), Données de séquences moléculaires, Hepacivirus (immunologie), Humains, Hépatite C (immunologie), Immunoglobuline G (immunologie), Lymphocytes B (immunologie), Protéines du core viral (immunologie), Protéines virales non structurales, Séquence d'acides aminés, Épitopes (analyse).
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence, Antibodies, Monoclonal (immunology), B-Lymphocytes (immunology), Capsid (immunology), Epitopes (analysis), Hepacivirus (immunology), Hepatitis C (immunology), Humans, Immunoglobulin G (immunology), Molecular Sequence Data, Viral Core Proteins (immunology), Viral Nonstructural Proteins.
- MESH :
- chemical , analysis : Epitopes.
- chemical , immunology : Antibodies, Monoclonal, Immunoglobulin G, Viral Core Proteins.
- immunology : B-Lymphocytes, Capsid, Hepacivirus, Hepatitis C.
- Amino Acid Sequence, Humans, Molecular Sequence Data, Viral Nonstructural Proteins.
Abstract
Several EBV-transformed B cell lines (BCL) were obtained from two patients with chronic hepatitis C virus (HCV) infection that secreted IgG class antibodies to the HCV nonstructural Ag c100-3. Two cloned BCL, derived from the same parental line, generated stable cloned lines that secreted up to 20 mg/liter of specific IgG1(kappa). Supernatants from oligoclonal and cloned BCL were also analyzed by immunoblot and all strongly reacted with recombinant polypeptides derived from the putative NS4 region of HCV, c100-3 and 5-1-1 (a 42-amino acid fragment of c100-3), whereas no reaction with the viral nucleoprotein, the NS3 nonstructural protein or the superoxide dismutase moiety of the c100-3 fusion protein could be documented. The fine specificity of these antibodies was also evaluated using overlapping synthetic peptides (20-mers) covering the 5-1-1 sequence. All oligoclonal and clonal IgG displayed high affinity binding to peptides covering residues 120-137 of Chiron's c100-3 sequence at the aminoterminus of 5-1-1. In addition, a minimal B cell epitope, N-VLYREF-C, was defined by human oligoclonal and monoclonal antibodies corresponding to residues 132-137. Interestingly, predominant recognition of the N-terminus of 5-1-1 was also observed in more than 80% of sera from patients with HCV infection. In conclusion, we have successfully produced human B cell cloned lines that secrete abundant quantities of IgG1(kappa)-specific for a polypeptide encoded by the NS4 region of HCV. Such antibodies recognize an immunodominant epitope, relative to this region, located at the N-terminus of the 5-1-1 fragment.
PubMed: 1717573
Affiliations:
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Le document en format XML
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Policlinico San Matteo, University of Pavia</wicri:regionArea><wicri:noRegion>University of Pavia</wicri:noRegion></affiliation></author><author><name sortKey="Mondelli, M U" sort="Mondelli, M U" uniqKey="Mondelli M" first="M U" last="Mondelli">M U Mondelli</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1717573</idno><idno type="pmid">1717573</idno><idno type="wicri:Area/PubMed/Corpus">002979</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002979</idno><idno type="wicri:Area/PubMed/Curation">002979</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002979</idno><idno type="wicri:Area/PubMed/Checkpoint">002839</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002839</idno><idno type="wicri:Area/Ncbi/Merge">000490</idno><idno type="wicri:Area/Ncbi/Curation">000490</idno><idno type="wicri:Area/Ncbi/Checkpoint">000490</idno><idno type="wicri:doubleKey">0022-1767:1991:Cerino A:identification:of:an</idno><idno type="wicri:Area/Main/Merge">004953</idno><idno type="wicri:Area/Main/Curation">004878</idno><idno type="wicri:Area/Main/Exploration">004878</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of an immunodominant B cell epitope on the hepatitis C virus nonstructural region defined by human monoclonal antibodies.</title><author><name sortKey="Cerino, A" sort="Cerino, A" uniqKey="Cerino A" first="A" last="Cerino">A. Cerino</name><affiliation wicri:level="1"><nlm:affiliation>Instituto di Clinica delle Malattie Infettive, I.R.C.C.S. Policlinico San Matteo, University of Pavia, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Instituto di Clinica delle Malattie Infettive, I.R.C.C.S. Policlinico San Matteo, University of Pavia</wicri:regionArea><wicri:noRegion>University of Pavia</wicri:noRegion></affiliation></author><author><name sortKey="Mondelli, M U" sort="Mondelli, M U" uniqKey="Mondelli M" first="M U" last="Mondelli">M U Mondelli</name></author></analytic><series><title level="j">Journal of immunology (Baltimore, Md. : 1950)</title><idno type="ISSN">0022-1767</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Antibodies, Monoclonal (immunology)</term><term>B-Lymphocytes (immunology)</term><term>Capsid (immunology)</term><term>Epitopes (analysis)</term><term>Hepacivirus (immunology)</term><term>Hepatitis C (immunology)</term><term>Humans</term><term>Immunoglobulin G (immunology)</term><term>Molecular Sequence Data</term><term>Viral Core Proteins (immunology)</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps monoclonaux (immunologie)</term><term>Capside (immunologie)</term><term>Données de séquences moléculaires</term><term>Hepacivirus (immunologie)</term><term>Humains</term><term>Hépatite C (immunologie)</term><term>Immunoglobuline G (immunologie)</term><term>Lymphocytes B (immunologie)</term><term>Protéines du core viral (immunologie)</term><term>Protéines virales non structurales</term><term>Séquence d'acides aminés</term><term>Épitopes (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Immunoglobulin G</term><term>Viral Core Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Capside</term><term>Hepacivirus</term><term>Hépatite C</term><term>Immunoglobuline G</term><term>Lymphocytes B</term><term>Protéines du core viral</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>B-Lymphocytes</term><term>Capsid</term><term>Hepacivirus</term><term>Hepatitis C</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Molecular Sequence Data</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Humains</term><term>Protéines virales non structurales</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Several EBV-transformed B cell lines (BCL) were obtained from two patients with chronic hepatitis C virus (HCV) infection that secreted IgG class antibodies to the HCV nonstructural Ag c100-3. Two cloned BCL, derived from the same parental line, generated stable cloned lines that secreted up to 20 mg/liter of specific IgG1(kappa). Supernatants from oligoclonal and cloned BCL were also analyzed by immunoblot and all strongly reacted with recombinant polypeptides derived from the putative NS4 region of HCV, c100-3 and 5-1-1 (a 42-amino acid fragment of c100-3), whereas no reaction with the viral nucleoprotein, the NS3 nonstructural protein or the superoxide dismutase moiety of the c100-3 fusion protein could be documented. The fine specificity of these antibodies was also evaluated using overlapping synthetic peptides (20-mers) covering the 5-1-1 sequence. All oligoclonal and clonal IgG displayed high affinity binding to peptides covering residues 120-137 of Chiron's c100-3 sequence at the aminoterminus of 5-1-1. In addition, a minimal B cell epitope, N-VLYREF-C, was defined by human oligoclonal and monoclonal antibodies corresponding to residues 132-137. Interestingly, predominant recognition of the N-terminus of 5-1-1 was also observed in more than 80% of sera from patients with HCV infection. In conclusion, we have successfully produced human B cell cloned lines that secrete abundant quantities of IgG1(kappa)-specific for a polypeptide encoded by the NS4 region of HCV. Such antibodies recognize an immunodominant epitope, relative to this region, located at the N-terminus of the 5-1-1 fragment.</div></front></TEI><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Mondelli, M U" sort="Mondelli, M U" uniqKey="Mondelli M" first="M U" last="Mondelli">M U Mondelli</name></noCountry><country name="Italie"><noRegion><name sortKey="Cerino, A" sort="Cerino, A" uniqKey="Cerino A" first="A" last="Cerino">A. Cerino</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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