Figure 6
Figure 6. AgAb can accommodate and efficiently elicit presentation of large viral antigens. (A) We fused fragments of EBNA3C with the C terminus of the Ig heavy chain that recognizes human CD21 and assessed their ability to induce specific T-cell recognition. Three AgAbs were thus generated with a 102-, 300-, or 963-bp fragment from the EBNA3C open reading frame, each of which include the 5H11 epitope. (B) The AgAbs were expressed in 293 cells and submitted to a western blot analysis using antibodies specific for mouse IgG proteins. Nontransfected 293 cells provided negative controls and anti-human CD20 antibody was used as a control for transfection. (C) The results of a T-cell assay performed in triplicate with 1 of the ex vivo–expanded 5H11-specific T-cell clones and LCLs loaded with the larger AgAbs. All assays were performed in triplicate and means and standard deviations are shown.

AgAb can accommodate and efficiently elicit presentation of large viral antigens. (A) We fused fragments of EBNA3C with the C terminus of the Ig heavy chain that recognizes human CD21 and assessed their ability to induce specific T-cell recognition. Three AgAbs were thus generated with a 102-, 300-, or 963-bp fragment from the EBNA3C open reading frame, each of which include the 5H11 epitope. (B) The AgAbs were expressed in 293 cells and submitted to a western blot analysis using antibodies specific for mouse IgG proteins. Nontransfected 293 cells provided negative controls and anti-human CD20 antibody was used as a control for transfection. (C) The results of a T-cell assay performed in triplicate with 1 of the ex vivo–expanded 5H11-specific T-cell clones and LCLs loaded with the larger AgAbs. All assays were performed in triplicate and means and standard deviations are shown.

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