Peptide selection by MHC class I molecules.
Synthetic peptides have been used to sensitize target cells and thereby screen for epitopes recognized by T cells. Most epitopes of cytotoxic T lymphocytes can be mimicked by synthetic peptides of 12-15 amino acids. Although in specific cases, truncations of peptides improves sensitization of target cells, no optimum length for binding to major histocompatibility complex (MHC) class I molecules has been defined. We have now analysed synthetic peptide captured by empty MHC class I molecules of the mutant cell line RMA-S. We found that class I molecules preferentially bound short peptides (nine amino acids) and selectively bound these peptides even when they were a minor component in a mixture of longer peptides. These results may help to explain the difference in size restriction of T-cell epitopes between experiments with synthetic peptides and those with naturally processed peptides.
Schumacher
T N
TN
Department of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam.
De Bruijn
M L
ML
Vernie
L N
LN
Kast
W M
WM
Melief
C J
CJ
Neefjes
J J
JJ
Ploegh
H L
HL
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D000939:Epitopes / Q000032:analysis / Q000276:immunology; D015395:Histocompatibility Antigens Class I / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000276:immunology; D011485:Protein Binding; D011925:Rauscher Virus / Q000235:genetics; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology
D000939:Epitopes; D015395:Histocompatibility Antigens Class I; D009842:Oligopeptides