Localization of hepatitis B surface antigen epitopes present on variants and specifically recognised by anti‐hepatitis B surface antigen monoclonal antibodies
Identifieur interne : 000239 ( France/Analysis ); précédent : 000238; suivant : 000240Localization of hepatitis B surface antigen epitopes present on variants and specifically recognised by anti‐hepatitis B surface antigen monoclonal antibodies
Auteurs : Colette Jolivet-Reynaud [France] ; Mylène Lésenéchal [France] ; Barbara O'Donnell [Royaume-Uni] ; Laurence Becquart [France] ; Agnès Foussadier [France] ; Françoise Forge [France] ; Nicole Battail-Poirot [France] ; Xavier Lacoux [France] ; William Carman [Royaume-Uni] ; Michel Jolivet [France]Source :
- Journal of Medical Virology [ 0146-6615 ] ; 2001-10.
English descriptors
- Teeft :
- Amino, Amino acid sequences, Amino acids, Assay, Biotinylated, Carman, Clone, Conformational epitopes, Culture supernatants, Cysteine residues, Determinant, Discontinuous epitopes, Dodecapeptide, Elisa, Epitope, Hbsag, Hbsag peptides, Hbsag sequence, Hbsag variants, Hepatitis, Hexapeptide, Identical residues, Immunoreactivity, Localisation, Mabs, Monoclonal antibodies, Mutant, Mutation, Nahco3 buffer, Nucleotide sequence, Peptide, Peptide libraries, Peptide library technology, Phage, Phage clones, Proc natl acad, Solid phase, Supernatant, Surface antigen, Triplicate, Variant, Virol, Virus surface antigen.
Abstract
Small hepatitis B surface antigen (HBsAg) is considered to be the best marker for the diagnosis of Hepatitis B virus infection. However, HBsAg variants with mutations within the “a” determinant may be poorly or not detected by diagnostic assays. Three anti‐HBsAg monoclonal antibodies (6H6B6, 27E7F10, and 2G2G10), directed against conformational epitopes, were tested for their ability to detect the wild‐type HBsAg as well as variant forms and their respective epitopes were localised on the HBsAg sequence by using the phage‐displayed peptide library technology. Whereas 6H6B6 did not detect mutations T123N, S143L, D144A and G145R, 27E7F10 binding was affected by mutations P120T and G145R. In contrast, 2G2G10 reacted strongly with all tested variants including variant with the G145R mutation. Part of the 6H6B6 epitope was located in the major hydrophilic region (MHR) at residues 101–105, the 27E7F10 epitope (residues 214–219) was located near the C‐terminal end of the antigen and the 2G2G10 epitope at residues 199–208, within the theoretical fourth transmembrane helix. The 2G2G10 epitope localisation brings information about the HBsAg structure and the validity of established topological models. Finally, 2G2G10 is a valuable tool for HBsAg variant detection that is used as capture phase in a new bioMérieux diagnostic assay, which is currently in development. J. Med. Virol. 65:241–249, 2001. © 2001 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jmv.2026
Affiliations:
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Scotland</wicri:regionArea><wicri:noRegion>Scotland</wicri:noRegion></affiliation></author><author><name sortKey="Jolivet, Michel" sort="Jolivet, Michel" uniqKey="Jolivet M" first="Michel" last="Jolivet">Michel Jolivet</name><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>bioMérieux, Département R & D unité Immunoessais, 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">65</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="241">241</biblScope><biblScope unit="page" to="249">249</biblScope><biblScope unit="page-count">9</biblScope><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-10">2001-10</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 sequences</term><term>Amino acids</term><term>Assay</term><term>Biotinylated</term><term>Carman</term><term>Clone</term><term>Conformational epitopes</term><term>Culture supernatants</term><term>Cysteine residues</term><term>Determinant</term><term>Discontinuous epitopes</term><term>Dodecapeptide</term><term>Elisa</term><term>Epitope</term><term>Hbsag</term><term>Hbsag peptides</term><term>Hbsag sequence</term><term>Hbsag variants</term><term>Hepatitis</term><term>Hexapeptide</term><term>Identical residues</term><term>Immunoreactivity</term><term>Localisation</term><term>Mabs</term><term>Monoclonal antibodies</term><term>Mutant</term><term>Mutation</term><term>Nahco3 buffer</term><term>Nucleotide sequence</term><term>Peptide</term><term>Peptide libraries</term><term>Peptide library technology</term><term>Phage</term><term>Phage clones</term><term>Proc natl acad</term><term>Solid phase</term><term>Supernatant</term><term>Surface antigen</term><term>Triplicate</term><term>Variant</term><term>Virol</term><term>Virus surface antigen</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Small hepatitis B surface antigen (HBsAg) is considered to be the best marker for the diagnosis of Hepatitis B virus infection. However, HBsAg variants with mutations within the “a” determinant may be poorly or not detected by diagnostic assays. Three anti‐HBsAg monoclonal antibodies (6H6B6, 27E7F10, and 2G2G10), directed against conformational epitopes, were tested for their ability to detect the wild‐type HBsAg as well as variant forms and their respective epitopes were localised on the HBsAg sequence by using the phage‐displayed peptide library technology. Whereas 6H6B6 did not detect mutations T123N, S143L, D144A and G145R, 27E7F10 binding was affected by mutations P120T and G145R. In contrast, 2G2G10 reacted strongly with all tested variants including variant with the G145R mutation. Part of the 6H6B6 epitope was located in the major hydrophilic region (MHR) at residues 101–105, the 27E7F10 epitope (residues 214–219) was located near the C‐terminal end of the antigen and the 2G2G10 epitope at residues 199–208, within the theoretical fourth transmembrane helix. The 2G2G10 epitope localisation brings information about the HBsAg structure and the validity of established topological models. Finally, 2G2G10 is a valuable tool for HBsAg variant detection that is used as capture phase in a new bioMérieux diagnostic assay, which is currently in development. J. Med. Virol. 65:241–249, 2001. © 2001 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>France</li><li>Royaume-Uni</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li><li>Écosse</li></region><settlement><li>Glasgow</li><li>Lyon</li></settlement><orgName><li>Université de Glasgow</li></orgName></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="Battail Oirot, Nicole" sort="Battail Oirot, Nicole" uniqKey="Battail Oirot N" first="Nicole" last="Battail-Poirot">Nicole Battail-Poirot</name><name sortKey="Becquart, Laurence" sort="Becquart, Laurence" uniqKey="Becquart L" first="Laurence" last="Becquart">Laurence Becquart</name><name sortKey="Forge, Francoise" sort="Forge, Francoise" uniqKey="Forge F" first="Françoise" last="Forge">Françoise Forge</name><name sortKey="Foussadier, Agnes" sort="Foussadier, Agnes" uniqKey="Foussadier A" first="Agnès" last="Foussadier">Agnès Foussadier</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="Jolivet, Michel" sort="Jolivet, Michel" uniqKey="Jolivet M" first="Michel" last="Jolivet">Michel Jolivet</name><name sortKey="Lacoux, Xavier" sort="Lacoux, Xavier" uniqKey="Lacoux X" first="Xavier" last="Lacoux">Xavier Lacoux</name><name sortKey="Lesenechal, Mylene" sort="Lesenechal, Mylene" uniqKey="Lesenechal M" first="Mylène" last="Lésenéchal">Mylène Lésenéchal</name></country><country name="Royaume-Uni"><region name="Écosse"><name sortKey="O Donnell, Barbara" sort="O Donnell, Barbara" uniqKey="O Donnell B" first="Barbara" last="O'Donnell">Barbara O'Donnell</name></region><name sortKey="Carman, William" sort="Carman, William" uniqKey="Carman W" first="William" last="Carman">William Carman</name><name sortKey="Carman, William" sort="Carman, William" uniqKey="Carman W" first="William" last="Carman">William Carman</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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