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*
Surgery Branch, Division of Clinical Sciences, and
Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892
To isolate melanoma Ags recognized by T cells, cDNA libraries made
from melanoma cell lines were screened with four CTLs derived from
tumor infiltrating lymphocytes (TIL) that were able to recognize
melanoma cells in a HLA-A1, -A2, or -A3 restricted manner. Although
cDNAs encoding the previously identified melanoma Ags, tyrosinase and
gp100, were isolated, these TIL were found to recognize previously
unidentified peptides. An HLA-A1-restricted CTL, TIL1388, was found to
recognize a tyrosinase peptide (SSDYVIPIGTY), and an HLA-A3-restricted
CTL, TIL1351, recognized a gp100 peptide (LIYRRRLMK). CTL clones
isolated from the HLA-A2-restricted TIL1383 recognized a gp100 peptide
(RLMKQDFSV). HLA-A2-restricted CTL, TIL1200, recognized a gp100 peptide
(RLPRIFCSC). Replacement of either cysteine residue with 
-amino
butyric acid in the gp100 peptide, RLPRIFCSC, enhanced CTL recognition,
suggesting that the peptide epitope naturally presented on the tumor
cell surface may contain reduced cysteine residues. Oxidation of these
cysteines might have occurred during the course of the synthesis or
pulsing of the peptide in culture. These modifications may have
important implications for the development of efficient peptide-based
vaccines. These newly identified peptide epitopes can extend the
ability to perform immunotherapy using synthetic peptides to a broader
population of patients, especially those expressing HLA-A1 or HLA-A3
for whom only a few melanoma epitopes have previously been
identified.
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