Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody.
Identifieur interne : 002708 ( PubMed/Curation ); précédent : 002707; suivant : 002709Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody.
Auteurs : A. Kramer [Allemagne] ; T. Keitel ; K. Winkler ; W. Stöcklein ; W. Höhne ; J. Schneider-MergenerSource :
- Cell [ 0092-8674 ] ; 1997.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Anticorps anti-VIH, Anticorps monoclonaux, Banque de peptides, Conformation des protéines, Données de séquences moléculaires, Fragments Fab d'immunoglobuline, Humains, Microscopie de fluorescence, Modèles moléculaires, Oligopeptides (), Protéine de capside p24 du VIH (), Protéine de capside p24 du VIH (immunologie), Sites de fixation des anticorps, Spécificité des anticorps, Séquence d'acides aminés, Test ELISA, Transfert d'énergie, VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie).
- MESH :
- immunologie : Protéine de capside p24 du VIH, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- Alignement de séquences, Animaux, Anticorps anti-VIH, Anticorps monoclonaux, Banque de peptides, Conformation des protéines, Données de séquences moléculaires, Fragments Fab d'immunoglobuline, Humains, Microscopie de fluorescence, Modèles moléculaires, Oligopeptides, Protéine de capside p24 du VIH, Sites de fixation des anticorps, Spécificité des anticorps, Séquence d'acides aminés, Test ELISA, Transfert d'énergie.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antibody Specificity, Binding Sites, Antibody, Energy Transfer, Enzyme-Linked Immunosorbent Assay, HIV Antibodies, HIV Core Protein p24 (chemistry), HIV Core Protein p24 (immunology), HIV-1 (immunology), Humans, Immunoglobulin Fab Fragments, Microscopy, Fluorescence, Models, Molecular, Molecular Sequence Data, Oligopeptides (chemistry), Peptide Library, Protein Conformation, Sequence Alignment.
- MESH :
- chemical , chemistry : HIV Core Protein p24, Oligopeptides.
- chemical , immunology : HIV Core Protein p24.
- chemical : Antibodies, Monoclonal, HIV Antibodies, Immunoglobulin Fab Fragments, Peptide Library.
- immunology : HIV-1.
- Amino Acid Sequence, Animals, Antibody Specificity, Binding Sites, Antibody, Energy Transfer, Enzyme-Linked Immunosorbent Assay, Humans, Microscopy, Fluorescence, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Alignment.
Abstract
Multiple binding capabilities utilized by specific protein-to-protein interactions in molecular recognition events are being documented increasingly but remain poorly understood at the molecular level. We identified five unrelated peptides that compete with each other for binding to the paratope region of the monoclonal anti-p24 (HIV-1) antibody CB4-1 by using a synthetic positional scanning combinatorial library XXXX[B1,B2,B3,X1,X2,X3]XXXX (14 mers; 68,590 peptide mixtures in total) prepared by spot synthesis. Complete sets of substitution analogs of the five peptides revealed key interacting residues, information that led to the construction of binding supertopes derived from each peptide. These supertope sequences were identified in hundreds of heterologous proteins, and those proteins that could be obtained were shown to bind CB4-1. Implications of these findings for immune escape mechanisms and autoimmunity are discussed.
DOI: 10.1016/s0092-8674(00)80468-7
PubMed: 9413989
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Stöcklein</name></author><author><name sortKey="Hohne, W" sort="Hohne, W" uniqKey="Hohne W" first="W" last="Höhne">W. Höhne</name></author><author><name sortKey="Schneider Mergener, J" sort="Schneider Mergener, J" uniqKey="Schneider Mergener J" first="J" last="Schneider-Mergener">J. 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Kramer</name><affiliation wicri:level="1"><nlm:affiliation>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin</wicri:regionArea></affiliation></author><author><name sortKey="Keitel, T" sort="Keitel, T" uniqKey="Keitel T" first="T" last="Keitel">T. Keitel</name></author><author><name sortKey="Winkler, K" sort="Winkler, K" uniqKey="Winkler K" first="K" last="Winkler">K. Winkler</name></author><author><name sortKey="Stocklein, W" sort="Stocklein, W" uniqKey="Stocklein W" first="W" last="Stöcklein">W. Stöcklein</name></author><author><name sortKey="Hohne, W" sort="Hohne, W" uniqKey="Hohne W" first="W" last="Höhne">W. 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We identified five unrelated peptides that compete with each other for binding to the paratope region of the monoclonal anti-p24 (HIV-1) antibody CB4-1 by using a synthetic positional scanning combinatorial library XXXX[B1,B2,B3,X1,X2,X3]XXXX (14 mers; 68,590 peptide mixtures in total) prepared by spot synthesis. Complete sets of substitution analogs of the five peptides revealed key interacting residues, information that led to the construction of binding supertopes derived from each peptide. These supertope sequences were identified in hundreds of heterologous proteins, and those proteins that could be obtained were shown to bind CB4-1. 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