An automated prediction of MHC class I-binding peptides based on positional scanning with peptide libraries
Identifieur interne : 003765 ( Main/Exploration ); précédent : 003764; suivant : 003766An automated prediction of MHC class I-binding peptides based on positional scanning with peptide libraries
Auteurs : Keiko Udaka [Japon] ; Karl-Heinz Wiesmüller [Allemagne] ; Stefan Kienle [Allemagne] ; Günther Jung [Allemagne] ; Hirokazu Tamamura [Japon] ; Hideo Yamagishi [Japon] ; Ko Okumura [Japon] ; Peter Walden [Allemagne] ; Taku Suto [Japon] ; Toshisuke Kawasaki [Japon]Source :
- Immunogenetics [ 0093-7711 ] ; 2000-08-01.
English descriptors
Abstract
Abstract.: Specificities of three mouse major histocompatibility complex (MHC) class I molecules, Kb, Db, and Ld, were analyzed by positional scanning using combinatorial peptide libraries. The result of the analysis was used to create a scoring program to predict MHC-binding peptides in proteins. The capacity of the scoring was then challenged with a number of peptides by comparing the prediction with the experimental binding. The score and the experimental binding exhibited a linear correlation but with substantial deviations of data points. Statistically, for approximately 80% of randomly chosen peptides, MHC-binding capacity could be predicted within one log concentration of peptides for a half-maximal binding. Known cytotoxic T-lymphocyte epitope peptides could be predicted, with a few exceptions. In addition, frequent findings of MHC-binding peptides with incomplete or no anchor amino acid(s) suggested a substantial bias introduced by natural antigen processing in peptide selection by MHC class I molecules.
Url:
DOI: 10.1007/s002510000217
Affiliations:
- Allemagne, Japon
- Bade-Wurtemberg, Berlin, District de Tübingen, Hambourg, Région de Kantō, Région du Kansai
- Berlin, Hambourg, Kyoto, Tokyo, Tübingen
- Université de Kyoto, Université de Tokyo
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Abstract.: Specificities of three mouse major histocompatibility complex (MHC) class I molecules, Kb, Db, and Ld, were analyzed by positional scanning using combinatorial peptide libraries. The result of the analysis was used to create a scoring program to predict MHC-binding peptides in proteins. The capacity of the scoring was then challenged with a number of peptides by comparing the prediction with the experimental binding. The score and the experimental binding exhibited a linear correlation but with substantial deviations of data points. Statistically, for approximately 80% of randomly chosen peptides, MHC-binding capacity could be predicted within one log concentration of peptides for a half-maximal binding. Known cytotoxic T-lymphocyte epitope peptides could be predicted, with a few exceptions. In addition, frequent findings of MHC-binding peptides with incomplete or no anchor amino acid(s) suggested a substantial bias introduced by natural antigen processing in peptide selection by MHC class I molecules.</div>
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