ZEH, HJ and LEDER, GH and LOTZE, MT and SALTER, RD and TECTOR, M and STUBER, G and MODROW, S and STORKUS, WJ (1994) FLOW-CYTOMETRIC DETERMINATION OF PEPTIDE CLASS-I COMPLEX-FORMATION - IDENTIFICATION OF P53 PEPTIDES THAT BIND TO HLA-A2. HUMAN IMMUNOLOGY, 39 (2). pp. 79-86. ISSN 0198-8859,
Full text not available from this repository.Abstract
A novel class I-peptide-binding assay was developed and used to identify a series of peptides derived from the human p53 tumor-suppressor gene product capable of binding the HLA-A2 class I allele. Brief pH 3.3 acid treatment of human cell lines rapidly denatures preexisting class I complexes, as detected by loss of binding of conformation-dependent mAbs, leaving only free class I heavy chains associated with the viable cell surface. These heavy chains may be induced to refold and be recognized by antibodies (in 2-4 hours) when acid-treated cells are coincubated with exogenous beta(2)-microglobulin and peptides capable of binding the relevant class I allele examined. This assay, with a detection limit of 1-10 nM peptide, was used to screen the capacity of a panel of nine peptides bearing HLA-A2-binding motifs and derived from the human p53 tumor-suppressor protein sequence. Eight of the nine peptides bound to, and reconstituted, HLA-A2 on acid-treated cells. This assay system will enable the rapid identification of peptides binding to any class I allele, which is the initial prerequisite for elucidating potential CD8 + T-cell epitopes.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MAJOR HISTOCOMPATIBILITY COMPLEX; MHC MOLECULES; LYMPHOCYTES-T; VIRUS PEPTIDES; CELLS; ANTIGEN; RECOGNITION; PROTEIN; GENE; ERADICATION; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53478 |
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