Characterization of antigenic peptides presented by HLA-B44 molecules on tumor cells expressing the gene MAGE-3

Katharina Fleischhauer, Doriana Fruci, Peter Van Endert, Jean Herman, Silvia Tanzarella, Hans J. Wallny, Pierre Coulie, Claudio Bordignon, Catia Traversari

Research output: Contribution to journalArticlepeer-review


The amino acid sequence of the protein encoded by the gene MAGE-3 was screened for peptides containing the binding motif for HLA-B44. Nine peptides were synthesized, and their binding affinity for HLA-B*4402 and -B*4403 was analyzed in an HLA class I α-chain refolding assay. Four peptides with binding affinity for HLA-B*4403 were chosen for in vitro cytotoxic T-lymphocyte induction assays using as antigen-presenting cells peptide-pulsed, autologous activated B lymphoblasts from a healthy, B*4403+ donor. Peptide-specific effecters could be raised only against one peptide, M3-167. Cytotoxic T lymphocytes specific for this peptide were also able to recognize melanoma cell lines expressing HLA-B44 and the gene MAGE-3, strongly suggesting that M3-167 is a naturally processed MAGE-3-encoded epitope presented by HLA-B44. M3-167 is a 1 amino acid N-terminal extension of M3-168, a naturally processed epitope MAGE-3-encoded epitope presented by HLA-A1 that has been previously described. TAP binding studies of these 2 peptides revealed that the TAP affinity of M3-167 is about 9-fold higher than that of M3-168. M3-167 or a longer precursor could be transported into the endoplasmatic reticulum, where it could be trimmed for presentation by HLA-A1 or -B44 molecules. Taken together, our data suggest that M3-167 could be an immunodominant peptide encoded by the gene MAGE-3.

Original languageEnglish
Pages (from-to)622-628
Number of pages7
JournalInternational Journal of Cancer
Issue number5
Publication statusPublished - 1996

ASJC Scopus subject areas

  • Cancer Research
  • Oncology


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