PMID: 9428921Jan 16, 1998Paper

HLA binding characteristics and generation of cytotoxic lymphocytes against peptides derived from oncogenic proteins

Tumori
C BertazzoliC Gambacorti-Passerini

Abstract

Structurally altered proteins (derived from chromosomal translocations or gene mutations) can be considered tumor specific antigens and represent an attractive target for a T-cell mediated response. T lymphocytes recognize antigens in the form of peptides bound to HLA-molecules. Peptides derived from oncogenic proteins were screened for the presence of HLA binding motifs; actual binding were evaluated by HLA stabilization experiments using transfectants and specific anti-HLA antibodies. Specific lymphocytes were induced by in vitro peptide sensitization and screened by thymidine uptake or cellular cytotoxic assays. We identified peptides derived from EWS/FLI-1 fusion protein and from mutated K-RAS protein (encompassing respectively the fusion point and the mutation at position 12) that showed binding motif for HLA-Cw*0702 and HLA-A3 respectively. The actual binding of these peptides was analysed in a stabilization assay. We detected binding for the EWS/FLI-1 peptide and for 5 RAS peptides (1 wild type and 4 mutated). The effect of temperature, beta 2-microglobulin (beta 2-m) and fetal calf serum (FCS) on the binding and the stability of the HLA/peptide complex was studied. A low temperature (26 degrees C) increased the binding ...Continue Reading

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