Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody
Identifieur interne : 001850 ( Istex/Corpus ); précédent : 001849; suivant : 001851Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody
Auteurs : Achim Kramer ; Thomas Keitel ; Karsten Winkler ; Walter Stöcklein ; Wolfgang Höhne ; Jens Schneider-MergenerSource :
- Cell [ 0092-8674 ] ; 1997.
English descriptors
- Teeft :
- Adjacent positions, Affinity, Alanine residues, Alcohol dehydrogenase, Amino, Amino acids, Antibody, Antibody binding, Antibody binding studies, Antibody polyspecificity, Association rate, Autoimmune diseases, Biacore measurements, Binding, Binding affinities, Binding experiments, Binding modes, Binding peptides, Binding promiscuity, Binding studies, Biotinylated peptides, Bovine serum albumin, Candidapepsin, Cellulose membranes, Coli, Combinatorial, Combinatorial libraries, Combinatorial peptide libraries, Competitive elisa, Complete regeneration, Complete sets, Continuous cellulose membranes, Corresponding proteins, Database, Database search, Database searches, Different binding modes, Different binding motifs, Different peptides, Dissociation constants, Elisa, Energy transfer, Epitope, Evaluation software, First screening step, Foreign pathogens, Generous gift, Heavy chain, Heterologous, Heterologous proteins, Hydrophobic contacts, Immunol, Inhibition constants, Jerini biotools gmbh, Keitel, Kramer, Light chain, Microtiter plates, Molecular basis, Molecular mimicry, Monoclonal, Monoclonal antibody, Mutant, Mutation, Natural antigen, Overall view, Peptide, Peptide epitope, Peptide gatpedlnqklagn, Peptide libraries, Peptide mixtures, Peptide sequences, Pinilla, Polymerase chain reaction, Polyspecificity, Positional scanning, Promiscuity, Protein regions, Protein samples, Rapid identification, Relevant peptide, Room temperature, Same region, Scfv, Scfv fragments, Single chain, Single substitution analogs, Small letters, Sodium carbonate buffer, Software pcgene, Soluble proteins, Spot synthesis, Strongest binding peptides, Structural basis, Structural requirements, Substantial loss, Substantial number, Substitution, Substitution analogs, Substitutional, Substitutional analyses, Substitutional analysis, Supertope, Supertope analysis, Supertope delineation, Supertope peptides, Supertopes, Total volume, Tryptophan residues, Umud, Umud protein, Unpublished data, Unrelated peptides, Variable regions, Various concentrations.
Abstract
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.
Url:
DOI: 10.1016/S0092-8674(00)80468-7
Links to Exploration step
ISTEX:C9559E952EA1497BFD096411604E6BD1BE470EFFLe document en format XML
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Germany</mods:affiliation></affiliation></author><author><name sortKey="Stocklein, Walter" sort="Stocklein, Walter" uniqKey="Stocklein W" first="Walter" last="Stöcklein">Walter Stöcklein</name><affiliation><mods:affiliation>Institut für Biochemie und Molekulare Physiologie, Universität Potsdam c/o Max-Delbrück-Centrum, Robert-Rössle-Straße 10, 13122 Berlin, Germany</mods:affiliation></affiliation></author><author><name sortKey="Hohne, Wolfgang" sort="Hohne, Wolfgang" uniqKey="Hohne W" first="Wolfgang" last="Höhne">Wolfgang Höhne</name><affiliation><mods:affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</mods:affiliation></affiliation></author><author><name sortKey="Schneider Mergener, Jens" sort="Schneider Mergener, Jens" uniqKey="Schneider Mergener J" first="Jens" last="Schneider-Mergener">Jens Schneider-Mergener</name><affiliation><mods:affiliation>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">91</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="799">799</biblScope><biblScope unit="page" to="809">809</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adjacent positions</term><term>Affinity</term><term>Alanine residues</term><term>Alcohol dehydrogenase</term><term>Amino</term><term>Amino acids</term><term>Antibody</term><term>Antibody binding</term><term>Antibody binding studies</term><term>Antibody polyspecificity</term><term>Association rate</term><term>Autoimmune diseases</term><term>Biacore measurements</term><term>Binding</term><term>Binding affinities</term><term>Binding experiments</term><term>Binding modes</term><term>Binding peptides</term><term>Binding promiscuity</term><term>Binding studies</term><term>Biotinylated peptides</term><term>Bovine serum albumin</term><term>Candidapepsin</term><term>Cellulose membranes</term><term>Coli</term><term>Combinatorial</term><term>Combinatorial libraries</term><term>Combinatorial peptide libraries</term><term>Competitive elisa</term><term>Complete regeneration</term><term>Complete sets</term><term>Continuous cellulose membranes</term><term>Corresponding proteins</term><term>Database</term><term>Database search</term><term>Database searches</term><term>Different binding modes</term><term>Different binding motifs</term><term>Different peptides</term><term>Dissociation constants</term><term>Elisa</term><term>Energy transfer</term><term>Epitope</term><term>Evaluation software</term><term>First screening step</term><term>Foreign pathogens</term><term>Generous gift</term><term>Heavy chain</term><term>Heterologous</term><term>Heterologous proteins</term><term>Hydrophobic contacts</term><term>Immunol</term><term>Inhibition constants</term><term>Jerini biotools gmbh</term><term>Keitel</term><term>Kramer</term><term>Light chain</term><term>Microtiter plates</term><term>Molecular basis</term><term>Molecular mimicry</term><term>Monoclonal</term><term>Monoclonal antibody</term><term>Mutant</term><term>Mutation</term><term>Natural antigen</term><term>Overall view</term><term>Peptide</term><term>Peptide epitope</term><term>Peptide gatpedlnqklagn</term><term>Peptide libraries</term><term>Peptide mixtures</term><term>Peptide sequences</term><term>Pinilla</term><term>Polymerase chain reaction</term><term>Polyspecificity</term><term>Positional 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residues</term><term>Umud</term><term>Umud protein</term><term>Unpublished data</term><term>Unrelated peptides</term><term>Variable regions</term><term>Various concentrations</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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. 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regeneration</json:string><json:string>antibody polyspecificity</json:string><json:string>supertope analysis</json:string><json:string>single substitution analogs</json:string></teeft></keywords><author><json:item><name>Achim Kramer</name><affiliations><json:string>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</json:string></affiliations></json:item><json:item><name>Thomas Keitel</name><affiliations><json:string>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</json:string></affiliations></json:item><json:item><name>Karsten Winkler</name><affiliations><json:string>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</json:string></affiliations></json:item><json:item><name>Walter Stöcklein</name><affiliations><json:string>Institut für Biochemie und Molekulare Physiologie, Universität Potsdam c/o Max-Delbrück-Centrum, Robert-Rössle-Straße 10, 13122 Berlin, Germany</json:string></affiliations></json:item><json:item><name>Wolfgang Höhne</name><affiliations><json:string>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</json:string></affiliations></json:item><json:item><name>Jens Schneider-Mergener</name><affiliations><json:string>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-HH8KLBH0-7</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>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.</abstract><qualityIndicators><score>8.548</score><pdfWordCount>7380</pdfWordCount><pdfCharCount>48224</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>129</abstractWordCount><abstractCharCount>951</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody</title><pmid><json:string>9413989</json:string></pmid><pii><json:string>S0092-8674(00)80468-7</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1997</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0082-7</json:string></pii><volume>91</volume><issue>6</issue><pages><first>799</first><last>809</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1997</json:string></date><geogName></geogName><orgName><json:string>AB</json:string><json:string>Novabiochem</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Walter Stocklein</json:string><json:string>Thomas Keitel</json:string><json:string>M. W. Kilimann</json:string><json:string>A. Guzzo</json:string><json:string>A. Arthur-Gottig</json:string><json:string>P. Adeberg</json:string><json:string>M. Monod</json:string><json:string>K. Winkler</json:string><json:string>A. Steinmetz</json:string><json:string>D. Volk</json:string><json:string>S. Jahn</json:string><json:string>D. Keßler</json:string><json:string>Wolfgang Hohne</json:string><json:string>P. Sullivan</json:string><json:string>H. Tanzmann</json:string><json:string>F. Melchers</json:string><json:string>Jens Schneider-Mergener</json:string><json:string>R. Stigler</json:string><json:string>M. Seifert</json:string><json:string>F. Endo</json:string><json:string>S. J. Lippard</json:string><json:string>Karsten Winkler</json:string><json:string>T. Formosa</json:string><json:string>P. A. Sullivan</json:string><json:string>C. Berek</json:string><json:string>E. D. Korn</json:string></persName><placeName><json:string>Polyspecificity</json:string><json:string>Berlin</json:string><json:string>Uppsala</json:string><json:string>Potsdam</json:string><json:string>Switzerland</json:string><json:string>Germany</json:string><json:string>Munich</json:string><json:string>Ulm</json:string><json:string>UK</json:string><json:string>Buckinghamshire</json:string><json:string>Mannheim</json:string><json:string>Maidstone</json:string><json:string>Bad Soden</json:string><json:string>Denmark</json:string><json:string>Frankfurt</json:string><json:string>United Kingdom</json:string><json:string>Sweden</json:string><json:string>Oxford</json:string><json:string>Roskilde</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Webster et al., 1994</json:string><json:string>Wing 1995</json:string><json:string>Needels et al., 1993</json:string><json:string>Friguet et al. 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(1995)</json:string><json:string>Orlandi et al., 1989</json:string><json:string>Arevalo et al., 1993</json:string><json:string>Peat et al., 1996</json:string><json:string>Geysen et al., 1988</json:string><json:string>Frank, 1992</json:string><json:string>Kramer et al., 1995</json:string><json:string>Hausdorf et al., 1994</json:string><json:string>Appel et al., 1996</json:string><json:string>Wucherpfennig and Strominger, 1995</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-HH8KLBH0-7</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - cell biology</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - developmental biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - General Biochemistry, Genetics and Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - embryologie: invertebres et vertebres. teratologie</json:string></inist></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1016/S0092-8674(00)80468-7</json:string></doi><id>C9559E952EA1497BFD096411604E6BD1BE470EFF</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-HH8KLBH0-7/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-HH8KLBH0-7/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-HH8KLBH0-7/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1997 Cell Press</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1997</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Article</note><note type="content">Figure 1: Substitutional Analyses of Library-Derived CB4-1 Binding Peptides Each residue of peptides 1–5 (Table 1) was substituted (rows) by all other (cysteine omitted) L- or D-amino acids (small letters) and analyzed for CB4-1 binding. The sequences corresponding to the left columns are identical and represent the starting peptide. Other spots are single substitution analogs. The exposure time was adjusted to approximate equal intensities in the left control columns. The relative spot intensities correlate qualitatively with the binding affinities (Volkmer-Engert et al. 1994).</note><note type="content">Figure 4: Conformations and Relative Orientations of Library-Derived Peptides 1, 2, and 5 in Complex with CB4-1 An overall view of the peptides GATPEDLNQKL (orange), GLYEWGGARIT (red), and the D-polymer lkGpl (green) binding to the cleft formed by the six complementarity determing loops of the monoclonal antibody CB4-1 (VH = heavy chain, VL = light chain; the left side of the peptides represent the N termini) is shown using the program ICM (Cardozo et al. 1995). In comparison to sequences given in Table 1, peptides 1, 2, and 5 are C- and/or N-terminally deleted, since no electron density could be seen for these residues (Keitel et al. 1997).</note><note type="content">Figure 2: CB4-1 Binding Studies with Database-Derived Peptides Matching Supertope 2 Peptide sequences (1219) matching supertope 2 were synthesized by spot synthesis in a 30 × 41 array and tested for CB4-1 binding. For comparison, the spots 1220–1230 correspond to peptide 2. Binding was visualized as described. The exposed X-ray film was scanned and quantified using the software IMAGEQUANT (Molecular Dynamics, Sunnyvale, California). The sequences of the 50 strongest binding peptides are given in Table 2.</note><note type="content">Figure 3: Dissociation Constants of CB4-1 Interacting with UmuD and Candiapepsin and Influences of CB4-1 Mutations on Peptide and Protein Recognition (A) Inhibition of CB4-1-p24 interaction by p24, UmuD, and candidapepsin determined by competitive ELISA. Soluble proteins compete with solid phase-adsorbed p24 for CB4-1 binding. 1/c (c = concentration of the inhibitors) is plotted versus E0/(E0-EX) (E = extinction with no inhibitor (0) and various inhibitor concentrations [x]). The slope of the fitted curves correspond to the inhibition constants (Friguet et al. 1985). (B) BIAcore measurements of UmuD interacting with solid phase-linked CB4-1. Overlay plot of various concentrations of UmuD (50 μM, 12.5 μM, 3.1 μM, and 0.78 μM [sensograms 1–4, respectively]) captured by CB4-1-coated chips. Samples were injected at t = 0 s. Dissociation started at t = 300 s. The association rate constant kon was determined as 3.0 × 103 M-1s-1, the dissociation rate constants koff as 6.0 × 103 s-1 resulting in Kd = 2.0 × 10−6 M. (C) CB4-1 single chain mutants VL:Phe94Ala and VH:Tyr32Ala as well as the wild-type CB4-1 single chain Fv fragment (wt) were tested for their ability to recognize immobilized peptide 1 (GATPEDLNQKLAGN) and peptide 2 (GLYEWGGARITNTD) as well as alcohol dehydrogenase (supertope 1-derived) and candidapepsin (supertope 2-derived). Binding of the CB4-1 single chains carrying the c-myc-tag were detected using the anti-c-myc antibody 9E10 and a peroxidase-conjugated anti-mouse antibody.</note><note type="content">Table 1: Identification and CB4-1 Binding of Library-Derived Peptides</note><note type="content">Table 2: CB4-1 Binding Peptides and Corresponding Proteins Identified by Supertope Analyses</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody</title><author xml:id="author-0000"><persName><forename type="first">Achim</forename><surname>Kramer</surname></persName><affiliation>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Thomas</forename><surname>Keitel</surname></persName><affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Karsten</forename><surname>Winkler</surname></persName><affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Walter</forename><surname>Stöcklein</surname></persName><affiliation>Institut für Biochemie und Molekulare Physiologie, Universität Potsdam c/o Max-Delbrück-Centrum, Robert-Rössle-Straße 10, 13122 Berlin, Germany</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Wolfgang</forename><surname>Höhne</surname></persName><affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation></author><author xml:id="author-0005"><persName><forename type="first">Jens</forename><surname>Schneider-Mergener</surname></persName><note type="biography">immunologie.charite.hu-berlin.de</note><note type="correspondence"><p>Correspondence: Jens Schneider-Mergener, 011-49-30-2802-6139 (phone), 011-49-30-2802-6480 (fax)</p></note><affiliation>immunologie.charite.hu-berlin.de</affiliation><affiliation>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation></author><idno type="istex">C9559E952EA1497BFD096411604E6BD1BE470EFF</idno><idno type="ark">ark:/67375/6H6-HH8KLBH0-7</idno><idno type="DOI">10.1016/S0092-8674(00)80468-7</idno><idno type="PII">S0092-8674(00)80468-7</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0082-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">91</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="799">799</biblScope><biblScope unit="page" to="809">809</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract></profileDesc><revisionDesc><change when="1997">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-HH8KLBH0-7/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity><istex:entity SYSTEM="gr5" NDATA="IMAGE" name="gr5"></istex:entity><istex:entity SYSTEM="gr6" NDATA="IMAGE" name="gr6"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>CELL</jid><aid>205</aid><ce:pii>S0092-8674(00)80468-7</ce:pii><ce:doi>10.1016/S0092-8674(00)80468-7</ce:doi><ce:copyright type="other" year="1997">Cell Press</ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody</ce:title><ce:author-group><ce:author><ce:given-name>Achim</ce:given-name><ce:surname>Kramer</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Thomas</ce:given-name><ce:surname>Keitel</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Karsten</ce:given-name><ce:surname>Winkler</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Walter</ce:given-name><ce:surname>Stöcklein</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Wolfgang</ce:given-name><ce:surname>Höhne</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jens</ce:given-name><ce:surname>Schneider-Mergener</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1">§</ce:cross-ref><ce:cross-ref refid="COR1">*</ce:cross-ref><ce:cross-ref refid="NEWFN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>1</ce:label><ce:textfn>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>2</ce:label><ce:textfn>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>3</ce:label><ce:textfn>Institut für Biochemie und Molekulare Physiologie, Universität Potsdam c/o Max-Delbrück-Centrum, Robert-Rössle-Straße 10, 13122 Berlin, Germany</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>*</ce:label><ce:text>Correspondence: Jens Schneider-Mergener, 011-49-30-2802-6139 (phone), 011-49-30-2802-6480 (fax)</ce:text></ce:correspondence><ce:footnote id="NEWFN1"><ce:label>1</ce:label><ce:note-para>immunologie.charite.hu-berlin.de</ce:note-para></ce:footnote></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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[B<ce:inf>1</ce:inf>,B<ce:inf>2</ce:inf>, B<ce:inf>3</ce:inf>,X<ce:inf>1</ce:inf>,X<ce:inf>2</ce:inf>,X<ce:inf>3</ce:inf>]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.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody</title></titleInfo><name type="personal"><namePart type="given">Achim</namePart><namePart type="family">Kramer</namePart><affiliation>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Thomas</namePart><namePart type="family">Keitel</namePart><affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Karsten</namePart><namePart type="family">Winkler</namePart><affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Walter</namePart><namePart type="family">Stöcklein</namePart><affiliation>Institut für Biochemie und Molekulare Physiologie, Universität Potsdam c/o Max-Delbrück-Centrum, Robert-Rössle-Straße 10, 13122 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Wolfgang</namePart><namePart type="family">Höhne</namePart><affiliation>Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jens</namePart><namePart type="family">Schneider-Mergener</namePart><affiliation>Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstraße 20-21, 10098 Berlin, Germany</affiliation><description>Correspondence: Jens Schneider-Mergener, 011-49-30-2802-6139 (phone), 011-49-30-2802-6480 (fax)</description><description>immunologie.charite.hu-berlin.de</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1997</dateIssued><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">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.</abstract><note type="content">Section title: Article</note><note type="content">Figure 1: Substitutional Analyses of Library-Derived CB4-1 Binding Peptides Each residue of peptides 1–5 (Table 1) was substituted (rows) by all other (cysteine omitted) L- or D-amino acids (small letters) and analyzed for CB4-1 binding. The sequences corresponding to the left columns are identical and represent the starting peptide. Other spots are single substitution analogs. The exposure time was adjusted to approximate equal intensities in the left control columns. The relative spot intensities correlate qualitatively with the binding affinities (Volkmer-Engert et al. 1994).</note><note type="content">Figure 4: Conformations and Relative Orientations of Library-Derived Peptides 1, 2, and 5 in Complex with CB4-1 An overall view of the peptides GATPEDLNQKL (orange), GLYEWGGARIT (red), and the D-polymer lkGpl (green) binding to the cleft formed by the six complementarity determing loops of the monoclonal antibody CB4-1 (VH = heavy chain, VL = light chain; the left side of the peptides represent the N termini) is shown using the program ICM (Cardozo et al. 1995). In comparison to sequences given in Table 1, peptides 1, 2, and 5 are C- and/or N-terminally deleted, since no electron density could be seen for these residues (Keitel et al. 1997).</note><note type="content">Figure 2: CB4-1 Binding Studies with Database-Derived Peptides Matching Supertope 2 Peptide sequences (1219) matching supertope 2 were synthesized by spot synthesis in a 30 × 41 array and tested for CB4-1 binding. For comparison, the spots 1220–1230 correspond to peptide 2. Binding was visualized as described. The exposed X-ray film was scanned and quantified using the software IMAGEQUANT (Molecular Dynamics, Sunnyvale, California). The sequences of the 50 strongest binding peptides are given in Table 2.</note><note type="content">Figure 3: Dissociation Constants of CB4-1 Interacting with UmuD and Candiapepsin and Influences of CB4-1 Mutations on Peptide and Protein Recognition (A) Inhibition of CB4-1-p24 interaction by p24, UmuD, and candidapepsin determined by competitive ELISA. Soluble proteins compete with solid phase-adsorbed p24 for CB4-1 binding. 1/c (c = concentration of the inhibitors) is plotted versus E0/(E0-EX) (E = extinction with no inhibitor (0) and various inhibitor concentrations [x]). The slope of the fitted curves correspond to the inhibition constants (Friguet et al. 1985). (B) BIAcore measurements of UmuD interacting with solid phase-linked CB4-1. Overlay plot of various concentrations of UmuD (50 μM, 12.5 μM, 3.1 μM, and 0.78 μM [sensograms 1–4, respectively]) captured by CB4-1-coated chips. Samples were injected at t = 0 s. Dissociation started at t = 300 s. The association rate constant kon was determined as 3.0 × 103 M-1s-1, the dissociation rate constants koff as 6.0 × 103 s-1 resulting in Kd = 2.0 × 10−6 M. (C) CB4-1 single chain mutants VL:Phe94Ala and VH:Tyr32Ala as well as the wild-type CB4-1 single chain Fv fragment (wt) were tested for their ability to recognize immobilized peptide 1 (GATPEDLNQKLAGN) and peptide 2 (GLYEWGGARITNTD) as well as alcohol dehydrogenase (supertope 1-derived) and candidapepsin (supertope 2-derived). Binding of the CB4-1 single chains carrying the c-myc-tag were detected using the anti-c-myc antibody 9E10 and a peroxidase-conjugated anti-mouse antibody.</note><note type="content">Table 1: Identification and CB4-1 Binding of Library-Derived Peptides</note><note type="content">Table 2: CB4-1 Binding Peptides and Corresponding Proteins Identified by Supertope Analyses</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1997</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0082-7</identifier><part><date>1997</date><detail type="volume"><number>91</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="issue-pages"><start>713</start><end>860</end></extent><extent unit="pages"><start>799</start><end>809</end></extent></part></relatedItem><identifier type="istex">C9559E952EA1497BFD096411604E6BD1BE470EFF</identifier><identifier type="ark">ark:/67375/6H6-HH8KLBH0-7</identifier><identifier type="DOI">10.1016/S0092-8674(00)80468-7</identifier><identifier type="PII">S0092-8674(00)80468-7</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Cell Press</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Cell Press, ©1997</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-HH8KLBH0-7/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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