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

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urn:nbn:de:bvb:355-epub-203959 Copy

Stuber, G. ; Leder, G. H. ; Storkus, W. T. ; Lotze, M. T. ; Modrow, Susanne ; Székely, L. ; Wolf, Hans J. ; Klein, E. ; Kärre, K. ; Klein, G.

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Date of publication of this fulltext: 06 Apr 2011 07:44

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Details

Item type:	Article
Journal or Publication Title:	European journal of immunology
Publisher:	Wiley-VCH
Volume:	24
Number of Issue or Book Chapter:	3
Page Range:	pp. 765-768
Date:	1994
Institutions:	Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene
Identification Number:	Value Type 8125143 PubMed ID 10.1002/eji.1830240341 DOI
Classification:	Notation Type 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 Decimal Classification:	600 Technology > 610 Medical sciences Medicine
Status:	Published
Refereed:	Unknown
Created at the University of Regensburg:	Unknown
Item ID:	20395

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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.

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