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Fig. 37 (abstract P297). | Journal for ImmunoTherapy of Cancer

Fig. 37 (abstract P297).

From: 31st Annual Meeting and Associated Programs of the Society for Immunotherapy of Cancer (SITC 2016): part two

Fig. 37 (abstract P297).

Alanine scanning to determine the key immunogenic AA residues of the H3.3.K27M epitope. a Relative HLA-A*0201-binding affinity of each peptide to that of H3.3.K27M (26–35) was determined by cell-free binding assay. b J.RT3-T3.5 cells were transduced with lentiviral vector encoding the H3.3.K27M-specific TCR and evaluated for the recognition of each peptide loaded on T2 cells by production of IL-2. Each group was assayed as triplicate *<0.05 by Student-t compared with the mutant H.3.3. In addition to 10 synthetic peptides each containing the substitution with alanine (A1-A10), we also evaluated synthetic peptides designed for citrullinated H3.3. K27M epitope (Cit H3.3; i.e., the first AA of the H3.3.K27M epitope is replaced by citrulline)

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