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T cell receptors recognize antigen peptides associated with major hitocompatibility complex (MHC) molecules on the antigen presenting cells (APC). Peptides bound to MHC class ‡T molecules, which are derived from intracellular pathogens or from proteins expressed in APC, are presented on the cell surface to the host immune system. Recently, peptides recognized by melanoma-specific cytotoxic T lymphocyte (CTL) have been identified from several melanoma-specific antigen-proteins using two alternative strategies. The first strategy has been to generate genomic or cDNA libraries from melanoma cells followed by transfection into cells which have the appropriate MHC molecule, and T cell epitopes containing antigenproteins are identified by their ability to reconstitute recognition by melanoma-specific CTL recognition. T cell epitope peptide is then confirmed by binding assay and cytotoxic assay using synthetic peptides based on the predicted sequence. In the second strategy, naturally occurring peptides associated with MHC molecules on the melanoma cells are directly extracted, separated by HPLC, and used to reconstitute recognition by melanoma-specific CTL of anonmelanoma cell expressing appropriate MHC molecules. The epitope peptide is purified from a reconstituting peptide containing fraction and sequenced by tandem mass spectrometry. Skipper et al. have identified the natural peptide target of the melanoma-specific CTL that recognizes the tyrosinase gene product of melanoma cells by using cDNA transfection strategy [Skipper, J. C. A., Hendrickson, R. C., Gulden, P. H., Brichard, V., Van Pel, A., Chen, Y.,Shabanowitz, J., Wolfel, T., Slingluff, C. L., Boon, T., Hunt, D. F., and Engelhard, V. H., (1996) J. Exp. Med. 183, 527-534]. The peptide YMDGTMSQV was identified by mass spectrometry as an HLA-A2.1 associated peptide. Surprisingly, YMDGTMSQV is not an encoded sequence of tyrosinase. The sequence of this peptide was identical to a nonamer peptide (YMDGTMSQV) corresponding to residue 368-376 of tyrosinase, except that aspartic acid (D) was found instead of asparagine (N) of the genetically encoded sequence (YMNGTMSQV). The peptide (YMDGTMSQV) is recognized by tyrosinase-specific CTL more effectively (100-fold) than the direct translation peptide (YMNGTMSQV) by using a target cell lysis assay. Since the T細 胞 受 容 体 は、抗 原提 示細 胞 (APC)上 の主 要組 織 適 合 遺

De-N-glycosylation Will Be the Novel Pathway for Processing of the Tumor Antigen Presented by MHC Class I