Figure 4
Figure 4. IFNγ+ T-cell responses to equimolar mixtures of 9-mer peptides identified by epitope mapping of in vitro responses and peptides within the same 15-mer or adjacent overlapping 15-mer peptides predicted to have higher binding affinity and immunogenicity. (A) Responses to a mixture of nonamers spanning amino acids +2 to +31 including the 6-15RDL and 22-31GGC peptides to which HLA A0201+ donors responded in epitope-mapping studies. (B) Responses to the in vitro–mapped (−75)-(−67)AILDFLLLQ epitope and a flanking peptide (−78)-(−70)LLAAILDFL with higher predicted binding affinity. (C) Responses to the in vitro–mapped 38-46LDFAPPGAS epitope and the overlapping 37-45VLDFAPPGA predicted to have higher binding affinity.

IFNγ+ T-cell responses to equimolar mixtures of 9-mer peptides identified by epitope mapping of in vitro responses and peptides within the same 15-mer or adjacent overlapping 15-mer peptides predicted to have higher binding affinity and immunogenicity. (A) Responses to a mixture of nonamers spanning amino acids +2 to +31 including the 6-15RDL and 22-31GGC peptides to which HLA A0201+ donors responded in epitope-mapping studies. (B) Responses to the in vitro–mapped (−75)-(−67)AILDFLLLQ epitope and a flanking peptide (−78)-(−70)LLAAILDFL with higher predicted binding affinity. (C) Responses to the in vitro–mapped 38-46LDFAPPGAS epitope and the overlapping 37-45VLDFAPPGA predicted to have higher binding affinity.

Close Modal

or Create an Account

Close Modal
Close Modal