Fig. 4.
Fig. 4. Characterization of the 12-mer peptide HIENFSDIDMGE as the minimal peptide sequence leading to maximal recognition by the HLA-DQ5 HY CTL. / Irradiated HLA-DQ5 female EBV cells were incubated with various concentrations (conc) of the indicated peptides for 2 hours. After washing, HLA-DQ5 HY CTLs were added; 16 hours later, supernatant was harvested and IFN-γ content was measured. Recognition considerably decreased after removal of the histidine residue on position 2, and further removal of N-terminal amino acids resulted in a further reduction of IFN-γ release by HLA-DQ5 HY CTL. Trimming of the C-terminal glutamic acid residue led to a slightly diminished recognition, while removal of the glycine residue completely abolished IFN-γ release by HLA-DQ5 HY CTL.

Characterization of the 12-mer peptide HIENFSDIDMGE as the minimal peptide sequence leading to maximal recognition by the HLA-DQ5 HY CTL.

Irradiated HLA-DQ5 female EBV cells were incubated with various concentrations (conc) of the indicated peptides for 2 hours. After washing, HLA-DQ5 HY CTLs were added; 16 hours later, supernatant was harvested and IFN-γ content was measured. Recognition considerably decreased after removal of the histidine residue on position 2, and further removal of N-terminal amino acids resulted in a further reduction of IFN-γ release by HLA-DQ5 HY CTL. Trimming of the C-terminal glutamic acid residue led to a slightly diminished recognition, while removal of the glycine residue completely abolished IFN-γ release by HLA-DQ5 HY CTL.

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