URN zum Zitieren dieses Dokuments: urn:nbn:de:bvb:355-epub-203959
Stuber, G., Leder, G. H., Storkus, W. T., Lotze, M. T., Modrow, Susanne, Székely, L., Wolf, Hans J., Klein, E., Kärre, K. und 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), S. 765-768.
Zum PubMed-Eintrag dieses Artikels
Zum Artikel beim Verlag (über DOI)
Zusammenfassung
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 ...
Zusammenfassung
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.
Bibliographische Daten exportieren
Dokumentenart: | Artikel |
---|
Datum: | 1994 |
---|
Institutionen: | Medizin > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
---|
Identifikationsnummer: | Wert | Typ |
---|
8125143 | PubMed-ID | 10.1002/eji.1830240341 | DOI |
|
---|
Klassifikation: | Notation | Art |
---|
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 |
|
---|
Dewey-Dezimal-Klassifikation: | 600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin |
---|
Status: | Veröffentlicht |
---|
Begutachtet: | Unbekannt / Keine Angabe |
---|
An der Universität Regensburg entstanden: | Unbekannt / Keine Angabe |
---|
Eingebracht am: | 06 Apr 2011 07:44 |
---|
Zuletzt geändert: | 08 Mrz 2017 08:29 |
---|
Dokumenten-ID: | 20395 |
---|