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

URN to cite this document:

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

DOI to cite this document:

10.5283/epub.20395 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.

Preview

PDF (392kB)

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

---

Alternative links to fulltext:PubmedDOI

---

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

Preview

Export bibliographical data

ASCII CitationAtomBibTeXData Cite XMLDataCite XML OAIDublin CoreDublin Core (LZV)EndNoteHTML CitationJSONJSON LDMETSMODSOPENAIREOpenAPCRDF+N-TriplesRDF+N3RDF+XMLReferReference ManagerSimple MetadataXMLopenCostxMetaDissPlus

---

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.

---

---

Metadata last modified: 29 Sep 2021 07:38

Owner only: item control page

Download Statistics

Download Statistics

Download Statistics

Download Statistics

Downloads

Downloads per month over past year

Altmetric

Altmetric

Altmetric

Alternative Statistics (altmetrics)

More literature (via CORE)

More literature (via CORE)

More literature (via CORE)

More literature (via CORE)