Figure 1.
Binding of the ESK2 clone no. 18 and no. 34 and specificity of the epitope. (A) Binding of clones to T2 cells pulsed with or without indicated peptides. WT1 RMF or mutant peptides at a concentration of 50 μg/mL were pulsed onto T2 cells overnight. Cells were washed and stained with BiTEs of ESK2 clone no. 18 and no. 34 or ESK1 at 1 μg/mL. T2 cells alone or pulsed with irrelevant HLA-A2–binding peptide HPV-E7 (39) were used as controls. (B) In parallel, HLA-A2 expression was determined by staining the cells with the anti–HLA-A2 mAb BB7 clone. (C) WT1 RMF sequences were substituted with alanine at positions 1, 3, 4, 5, 7, and 8, or with glycine at position 6 indicated as WT1-A1 to WT1-A8 or WT1-G6, respectively (supplemental Table 1) and the binding of (C) ESK2-clone no. 18 and no. 34 and (D) HLA-A2 was determined by flow cytometric analysis. The data are representative results from 6 similar experiments. HPV, human papilloma virus.

Binding of the ESK2 clone no. 18 and no. 34 and specificity of the epitope. (A) Binding of clones to T2 cells pulsed with or without indicated peptides. WT1 RMF or mutant peptides at a concentration of 50 μg/mL were pulsed onto T2 cells overnight. Cells were washed and stained with BiTEs of ESK2 clone no. 18 and no. 34 or ESK1 at 1 μg/mL. T2 cells alone or pulsed with irrelevant HLA-A2–binding peptide HPV-E7 (39) were used as controls. (B) In parallel, HLA-A2 expression was determined by staining the cells with the anti–HLA-A2 mAb BB7 clone. (C) WT1 RMF sequences were substituted with alanine at positions 1, 3, 4, 5, 7, and 8, or with glycine at position 6 indicated as WT1-A1 to WT1-A8 or WT1-G6, respectively (supplemental Table 1) and the binding of (C) ESK2-clone no. 18 and no. 34 and (D) HLA-A2 was determined by flow cytometric analysis. The data are representative results from 6 similar experiments. HPV, human papilloma virus.

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