Binding affinity independent contribution of peptide length to the stability of peptide-HLA-DR complexes in live antigen presenting cells
The effect of peptide length on the stability of peptide-HLR-DR1 (DR1) complexes was analyzed using two peptide series of increasing length, each containing a 7mer core with five DR1-binding anchors, extended stepwise with A1a residues at the N- and C-terminus, respectively. The A1a extensions, alth...
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| Veröffentlicht in: | Human immunology 1998-08, Vol.59 (8), p.463-471 |
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| container_title | Human immunology |
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| creator | Siklodi, Botond Vogt, Anne B Kropshofer, Harald Falcioni, Fiorenza Molina, Margarita Bolin, David R Campbell, Robert Hämmerling, Günter J Nagy, Zoltan A |
| description | The effect of peptide length on the stability of peptide-HLR-DR1 (DR1) complexes was analyzed using two peptide series of increasing length, each containing a 7mer core with five DR1-binding anchors, extended stepwise with A1a residues at the N- and C-terminus, respectively. The A1a extensions, although did not affect binding affinity, significantly increased the half lives of peptide-DR1 complexes (from 1.5 h up to 10 h) in live antigen presenting cells (APC). Flanking residues from position −2 to 0 and 8 to 11 were involved in the affinity-independent increase of complex stability. The shortest (8mer and 9mer) peptides, with
in vivo half lives of 9 residues, and the longevity of complexes seems to depend on full of occupation of the binding site. |
| doi_str_mv | 10.1016/S0198-8859(98)00038-X |
| format | Article |
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in vivo half lives of <2.5 h, were unable to form stable complexes with DR1 in presence of HLA-DM (DM) molecules, and were poor competitors of antigen presentation. Longer peptides were resistant to DM-mediated unloading, and were efficient competitors of antigen presentation. Thus, DM appears to limit short peptides in establishing biologically relevant DR occupancy, despite their high binding affinity. In APC, stable complexes can form only with high affinity peptides of >9 residues, and the longevity of complexes seems to depend on full of occupation of the binding site.</description><identifier>ISSN: 0198-8859</identifier><identifier>EISSN: 1879-1166</identifier><identifier>DOI: 10.1016/S0198-8859(98)00038-X</identifier><identifier>PMID: 9712349</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Antibodies, Monoclonal ; Antigen Presentation ; Antigen-Presenting Cells - immunology ; Binding Sites ; Cell Line, Transformed ; Half-Life ; Histocompatibility Antigens Class II ; HLA-D Antigens - immunology ; HLA-DR1 Antigen - metabolism ; Humans ; Lymphocyte Activation ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Peptide Fragments - chemistry ; T-Lymphocytes - immunology</subject><ispartof>Human immunology, 1998-08, Vol.59 (8), p.463-471</ispartof><rights>1998 American Society for Histocompatibility and Immunogenetics</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-9afc0a1183394d5a1f6f540570f61ad3a922e0ebdb5c64d65ecc95e638aa62043</citedby><cites>FETCH-LOGICAL-c391t-9afc0a1183394d5a1f6f540570f61ad3a922e0ebdb5c64d65ecc95e638aa62043</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0198-8859(98)00038-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9712349$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siklodi, Botond</creatorcontrib><creatorcontrib>Vogt, Anne B</creatorcontrib><creatorcontrib>Kropshofer, Harald</creatorcontrib><creatorcontrib>Falcioni, Fiorenza</creatorcontrib><creatorcontrib>Molina, Margarita</creatorcontrib><creatorcontrib>Bolin, David R</creatorcontrib><creatorcontrib>Campbell, Robert</creatorcontrib><creatorcontrib>Hämmerling, Günter J</creatorcontrib><creatorcontrib>Nagy, Zoltan A</creatorcontrib><title>Binding affinity independent contribution of peptide length to the stability of peptide-HLA-DR complexes in live antigen presenting cells</title><title>Human immunology</title><addtitle>Hum Immunol</addtitle><description>The effect of peptide length on the stability of peptide-HLR-DR1 (DR1) complexes was analyzed using two peptide series of increasing length, each containing a 7mer core with five DR1-binding anchors, extended stepwise with A1a residues at the N- and C-terminus, respectively. The A1a extensions, although did not affect binding affinity, significantly increased the half lives of peptide-DR1 complexes (from 1.5 h up to 10 h) in live antigen presenting cells (APC). Flanking residues from position −2 to 0 and 8 to 11 were involved in the affinity-independent increase of complex stability. The shortest (8mer and 9mer) peptides, with
in vivo half lives of <2.5 h, were unable to form stable complexes with DR1 in presence of HLA-DM (DM) molecules, and were poor competitors of antigen presentation. Longer peptides were resistant to DM-mediated unloading, and were efficient competitors of antigen presentation. Thus, DM appears to limit short peptides in establishing biologically relevant DR occupancy, despite their high binding affinity. In APC, stable complexes can form only with high affinity peptides of >9 residues, and the longevity of complexes seems to depend on full of occupation of the binding site.</description><subject>Antibodies, Monoclonal</subject><subject>Antigen Presentation</subject><subject>Antigen-Presenting Cells - immunology</subject><subject>Binding Sites</subject><subject>Cell Line, Transformed</subject><subject>Half-Life</subject><subject>Histocompatibility Antigens Class II</subject><subject>HLA-D Antigens - immunology</subject><subject>HLA-DR1 Antigen - metabolism</subject><subject>Humans</subject><subject>Lymphocyte Activation</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Peptide Fragments - chemistry</subject><subject>T-Lymphocytes - immunology</subject><issn>0198-8859</issn><issn>1879-1166</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV1rHCEYhSWkJNu0PyHgVUkuptV1dPSqJNuPFBYK_YDciaOvG8usM1U3ND-h_7pOdkkvc-OLvM85RzwInVPylhIq3n0nVMlGSq4ulLwkhDDZ3B6hBZWdaigV4hgtnpBT9DLnXxXqSNeeoBPV0SVr1QL9vQ7RhbjBxvsQQ3nA9Q4T1CMWbMdYUuh3JYwRjx5PMJXgAA8QN-UOlxGXO8C5mD4Ms_Y_0tysr5oP36rDdhrgD-Tqi4dwD9jEEjYQ8ZQg14w528Iw5FfohTdDhteHeYZ-fvr4Y3XTrL9-_rK6WjeWKVoaZbwlhlLJmGodN9QLz1vCO-IFNY4ZtVwCgd713IrWCQ7WKg6CSWPEkrTsDL3Z-05p_L2DXPQ25PkFJsK4y7pjksu2Y8-CVLRKMC4qyPegTWPOCbyeUtia9KAp0XNX-rErPReh63zsSt9W3fkhYNdvwT2pDuXU_fv9Hup33AdIOtsA0YILCWzRbgzPJPwDVjKmuw</recordid><startdate>19980801</startdate><enddate>19980801</enddate><creator>Siklodi, Botond</creator><creator>Vogt, Anne B</creator><creator>Kropshofer, Harald</creator><creator>Falcioni, Fiorenza</creator><creator>Molina, Margarita</creator><creator>Bolin, David R</creator><creator>Campbell, Robert</creator><creator>Hämmerling, Günter J</creator><creator>Nagy, Zoltan A</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19980801</creationdate><title>Binding affinity independent contribution of peptide length to the stability of peptide-HLA-DR complexes in live antigen presenting cells</title><author>Siklodi, Botond ; 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The A1a extensions, although did not affect binding affinity, significantly increased the half lives of peptide-DR1 complexes (from 1.5 h up to 10 h) in live antigen presenting cells (APC). Flanking residues from position −2 to 0 and 8 to 11 were involved in the affinity-independent increase of complex stability. The shortest (8mer and 9mer) peptides, with
in vivo half lives of <2.5 h, were unable to form stable complexes with DR1 in presence of HLA-DM (DM) molecules, and were poor competitors of antigen presentation. Longer peptides were resistant to DM-mediated unloading, and were efficient competitors of antigen presentation. Thus, DM appears to limit short peptides in establishing biologically relevant DR occupancy, despite their high binding affinity. In APC, stable complexes can form only with high affinity peptides of >9 residues, and the longevity of complexes seems to depend on full of occupation of the binding site.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9712349</pmid><doi>10.1016/S0198-8859(98)00038-X</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0198-8859 |
| ispartof | Human immunology, 1998-08, Vol.59 (8), p.463-471 |
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| subjects | Antibodies, Monoclonal Antigen Presentation Antigen-Presenting Cells - immunology Binding Sites Cell Line, Transformed Half-Life Histocompatibility Antigens Class II HLA-D Antigens - immunology HLA-DR1 Antigen - metabolism Humans Lymphocyte Activation Oligopeptides - chemistry Oligopeptides - metabolism Peptide Fragments - chemistry T-Lymphocytes - immunology |
| title | Binding affinity independent contribution of peptide length to the stability of peptide-HLA-DR complexes in live antigen presenting cells |
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