Stuber, G., Leder, G. H., Storkus, W. T., Lotze, M. T., Modrow, Susanne, Székely, L., Wolf, Hans J., Klein, E., Kärre, K. and Klein, G.
(1994)
Identification of wild-type and mutant p53 peptides binding to HLA-A2 assessed by a peptide loading-deficient cell line assay and a novel major histocompatibility complex class I peptide binding assay.
European journal of immunology 24 (3), pp. 765-768.
Date of publication of this fulltext: 06 Apr 2011 07:44at PubMed
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Abstract
Mutations of the p53 gene are the most frequently observed genetic changes in human cancers; often leading to an overexpression of the wild-type (wt) p53 protein. Demonstrable T cell reactivity against tumor cells overexpressing wt or mutant p53-derived peptides could support the application of such epitopes in cancer immunotherapies. As the binding of peptide to MHC class I molecules is a ...
Abstract
Mutations of the p53 gene are the most frequently observed genetic changes in human cancers; often leading to an overexpression of the wild-type (wt) p53 protein. Demonstrable T cell reactivity against tumor cells overexpressing wt or mutant p53-derived peptides could support the application of such epitopes in cancer immunotherapies. As the binding of peptide to MHC class I molecules is a prerequisite for antigen-specific T cell recognition, we evaluated the ability of wt and mutant p53 peptides to bind to HLA-A2.1 using two independent flow cytometry-based assay systems, the T2 major histocompatibility complex (MHC) class I peptide stabilization assay (stabilization assay) and the peptide-induced MHC class I reconstitution assay (reconstitution assay). The twenty selected wt sequences each conformed to the previously reported HLA-A2.1 peptide binding motif. Seven of the wt p53 and 2/13 mutant p53 peptides derived from the previously chosen wt peptides bound to HLA-A2.1 in both the stabilization and the reconstitution assays. An additional six wt and six mutant p53 peptides, presumably exhibiting lower affinity for HLA-A2.1, were identified only in the reconstitution assay. Those p53 peptides binding HLA-A2.1 may provide useful immunogens for the generation of HLA-A2.1-restricted cytolytic T lymphocytes in vitro and in vivo.
Export bibliographical data
| Item type: | Article |
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| Date: | 1994 |
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| Institutions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
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| Identification Number: | | Value | Type |
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| 8125143 | PubMed ID | | 10.1002/eji.1830240341 | DOI |
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| Classification: | | Notation | Type |
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| Amino Acid Sequence | MESH | | Cell Line | MESH | | HLA-A2 Antigen/immunology | MESH | | Humans | MESH | | Molecular Sequence Data | MESH | | Peptides/immunology | MESH | | Protein Binding | MESH | | Structure-Activity Relationship | MESH | | Tumor Suppressor Protein p53/immunology | MESH |
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| Dewey Decimal Classification: | 600 Technology > 610 Medical sciences Medicine |
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| Status: | Published |
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| Refereed: | Unknown |
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| Created at the University of Regensburg: | Unknown |
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| Item ID: | 20395 |
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