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CD8 T lymphocytes recognize peptides of 8 to 10 amino acids presented by class I molecules of the major histocompatibility complex. Here, CD8 T lymphocytes were found to recognize a nonameric peptide on melanoma cells that comprises two noncontiguous segments of melanocytic glycoprotein gp100(PMEL17). The production of this peptide involves the excision of four amino acids and splicing of the fragments. This process was reproduced in vitro by incubating a precursor peptide of 13 amino acids with highly purified proteasomes. Splicing appears to occur by transpeptidation involving an acyl-enzyme intermediate. Our results reveal an unanticipated aspect of the proteasome function of producing antigenic peptides.

Original publication

DOI

10.1126/science.1095522

Type

Journal article

Journal

Science

Publication Date

23/04/2004

Volume

304

Pages

587 - 590

Keywords

Animals, Antigen Presentation, COS Cells, Cell Line, Tumor, Cysteine Endopeptidases, Electroporation, HLA-A Antigens, Humans, Interferon-gamma, Melanoma, Membrane Glycoproteins, Models, Chemical, Multienzyme Complexes, Neoplasm Proteins, Peptide Fragments, Proteasome Endopeptidase Complex, Protein Precursors, Protein Splicing, T-Lymphocytes, Cytotoxic, Transfection, gp100 Melanoma Antigen