Characterization of oligopeptides that cross-react with carbohydrate-specific antibodies by real time kinetics, in-solution competition enzyme-linked immunosorbent assay, and immunological analyses.
Identifieur interne : 003341 ( Main/Exploration ); précédent : 003340; suivant : 003342Characterization of oligopeptides that cross-react with carbohydrate-specific antibodies by real time kinetics, in-solution competition enzyme-linked immunosorbent assay, and immunological analyses.
Auteurs : Paul J. Brett ; Harmale Tiwana ; Ian M. Feavers ; Bambos M. CharalambousSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2002.
Descripteurs français
- KwdFr :
- ADN viral, Animaux, Anticorps monoclonaux (), Anticorps monoclonaux (immunologie), Bactériophages (génétique), Cinétique, Lipopolysaccharides (immunologie), Mimétisme moléculaire, Neisseria meningitidis (immunologie), Oligopeptides (immunologie), Réactions croisées, Similitude de séquences d'acides nucléiques, Souris, Souris de lignée C3H, Séquence d'acides aminés, Séquence nucléotidique, Test ELISA (), Épitopes (), Épitopes (immunologie).
- MESH :
- génétique : Bactériophages.
- immunologie : Anticorps monoclonaux, Lipopolysaccharides, Neisseria meningitidis, Oligopeptides, Épitopes.
- ADN viral, Animaux, Anticorps monoclonaux, Cinétique, Mimétisme moléculaire, Réactions croisées, Similitude de séquences d'acides nucléiques, Souris, Souris de lignée C3H, Séquence d'acides aminés, Séquence nucléotidique, Test ELISA, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (chemistry), Antibodies, Monoclonal (immunology), Bacteriophages (genetics), Base Sequence, Cross Reactions, DNA, Viral, Enzyme-Linked Immunosorbent Assay (methods), Epitopes (chemistry), Epitopes (immunology), Kinetics, Lipopolysaccharides (immunology), Mice, Mice, Inbred C3H, Molecular Mimicry, Neisseria meningitidis (immunology), Oligopeptides (immunology), Sequence Homology, Nucleic Acid.
- MESH :
- chemical , chemistry : Antibodies, Monoclonal, Epitopes.
- chemical , immunology : Antibodies, Monoclonal, Epitopes, Lipopolysaccharides, Oligopeptides.
- genetics : Bacteriophages.
- immunology : Neisseria meningitidis.
- methods : Enzyme-Linked Immunosorbent Assay.
- Amino Acid Sequence, Animals, Base Sequence, Cross Reactions, DNA, Viral, Kinetics, Mice, Mice, Inbred C3H, Molecular Mimicry, Sequence Homology, Nucleic Acid.
Abstract
Phage displaying random cyclic 7-mer, and linear 7-mer and 12-mer peptides at the N terminus of the coat protein, pIII, were panned with the murine monoclonal antibody, 9-2-L379 specific for meningococcal lipo-oligosaccharide. Five cyclic peptides with two sequence motifs, six linear 7-mers, and five linear 12-mers with different sequence motifs were identified. Only phage displaying cyclic peptides were specifically captured by and were antigenic for 9-2-L379. Monoclonal antibody 9-2-L379 exhibited "apparent" binding affinities to the cyclic peptides between 11 and 184 nm, comparable with lipo-oligosaccharide. All cyclic peptides competed with the binding of 9-2-L379 to lipo-oligosaccharide with EC(50) values in the range 10-105 microm, which correlated with their apparent binding affinities. Structural modifications of the cyclic peptides eliminated their ability to bind and compete with monoclonal antibody 9-2-L379. Mice (C3H/HeN) immunized with the cyclic peptide with optimal apparent binding affinity and EC(50) of competition elicited cross-reactive antibodies to meningococcal lipo-oligosaccharide with end point dilution serum antibody titers of 3200. Cyclic peptides were converted to T-cell-dependent immunogens without disrupting these properties by C-terminal biotinylation and complexing with NeutrAvidin. The data indicate that constrained peptides can cross-react with a carbohydrate-specific antibody with greater specificity than linear peptides, and critical to this specificity is their structural conformation.
DOI: 10.1074/jbc.M200387200
PubMed: 11923297
Affiliations:
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Le document en format XML
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Feavers</name></author><author><name sortKey="Charalambous, Bambos M" sort="Charalambous, Bambos M" uniqKey="Charalambous B" first="Bambos M" last="Charalambous">Bambos M. 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Brett</name><affiliation><nlm:affiliation>Department of Medical Microbiology, Royal Free and University College Medical School, Royal Free Campus, University College London, Rowland Hill Street, London NW3 2PF.</nlm:affiliation><wicri:noCountry code="subField">London NW3 2PF</wicri:noCountry></affiliation></author><author><name sortKey="Tiwana, Harmale" sort="Tiwana, Harmale" uniqKey="Tiwana H" first="Harmale" last="Tiwana">Harmale Tiwana</name></author><author><name sortKey="Feavers, Ian M" sort="Feavers, Ian M" uniqKey="Feavers I" first="Ian M" last="Feavers">Ian M. Feavers</name></author><author><name sortKey="Charalambous, Bambos M" sort="Charalambous, Bambos M" uniqKey="Charalambous B" first="Bambos M" last="Charalambous">Bambos M. Charalambous</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibodies, Monoclonal (chemistry)</term><term>Antibodies, Monoclonal (immunology)</term><term>Bacteriophages (genetics)</term><term>Base Sequence</term><term>Cross Reactions</term><term>DNA, Viral</term><term>Enzyme-Linked Immunosorbent Assay (methods)</term><term>Epitopes (chemistry)</term><term>Epitopes (immunology)</term><term>Kinetics</term><term>Lipopolysaccharides (immunology)</term><term>Mice</term><term>Mice, Inbred C3H</term><term>Molecular Mimicry</term><term>Neisseria meningitidis (immunology)</term><term>Oligopeptides (immunology)</term><term>Sequence Homology, Nucleic Acid</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN viral</term><term>Animaux</term><term>Anticorps monoclonaux ()</term><term>Anticorps monoclonaux (immunologie)</term><term>Bactériophages (génétique)</term><term>Cinétique</term><term>Lipopolysaccharides (immunologie)</term><term>Mimétisme moléculaire</term><term>Neisseria meningitidis (immunologie)</term><term>Oligopeptides (immunologie)</term><term>Réactions croisées</term><term>Similitude de séquences d'acides nucléiques</term><term>Souris</term><term>Souris de lignée C3H</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Test ELISA ()</term><term>Épitopes ()</term><term>Épitopes (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Epitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Epitopes</term><term>Lipopolysaccharides</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bacteriophages</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Bactériophages</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Lipopolysaccharides</term><term>Neisseria meningitidis</term><term>Oligopeptides</term><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Neisseria meningitidis</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Enzyme-Linked Immunosorbent Assay</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cross Reactions</term><term>DNA, Viral</term><term>Kinetics</term><term>Mice</term><term>Mice, Inbred C3H</term><term>Molecular Mimicry</term><term>Sequence Homology, Nucleic Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN viral</term><term>Animaux</term><term>Anticorps monoclonaux</term><term>Cinétique</term><term>Mimétisme moléculaire</term><term>Réactions croisées</term><term>Similitude de séquences d'acides nucléiques</term><term>Souris</term><term>Souris de lignée C3H</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Test ELISA</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phage displaying random cyclic 7-mer, and linear 7-mer and 12-mer peptides at the N terminus of the coat protein, pIII, were panned with the murine monoclonal antibody, 9-2-L379 specific for meningococcal lipo-oligosaccharide. Five cyclic peptides with two sequence motifs, six linear 7-mers, and five linear 12-mers with different sequence motifs were identified. Only phage displaying cyclic peptides were specifically captured by and were antigenic for 9-2-L379. Monoclonal antibody 9-2-L379 exhibited "apparent" binding affinities to the cyclic peptides between 11 and 184 nm, comparable with lipo-oligosaccharide. All cyclic peptides competed with the binding of 9-2-L379 to lipo-oligosaccharide with EC(50) values in the range 10-105 microm, which correlated with their apparent binding affinities. Structural modifications of the cyclic peptides eliminated their ability to bind and compete with monoclonal antibody 9-2-L379. Mice (C3H/HeN) immunized with the cyclic peptide with optimal apparent binding affinity and EC(50) of competition elicited cross-reactive antibodies to meningococcal lipo-oligosaccharide with end point dilution serum antibody titers of 3200. Cyclic peptides were converted to T-cell-dependent immunogens without disrupting these properties by C-terminal biotinylation and complexing with NeutrAvidin. The data indicate that constrained peptides can cross-react with a carbohydrate-specific antibody with greater specificity than linear peptides, and critical to this specificity is their structural conformation.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Brett, Paul J" sort="Brett, Paul J" uniqKey="Brett P" first="Paul J" last="Brett">Paul J. Brett</name><name sortKey="Charalambous, Bambos M" sort="Charalambous, Bambos M" uniqKey="Charalambous B" first="Bambos M" last="Charalambous">Bambos M. Charalambous</name><name sortKey="Feavers, Ian M" sort="Feavers, Ian M" uniqKey="Feavers I" first="Ian M" last="Feavers">Ian M. Feavers</name><name sortKey="Tiwana, Harmale" sort="Tiwana, Harmale" uniqKey="Tiwana H" first="Harmale" last="Tiwana">Harmale Tiwana</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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