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The present work was designed to compare two mechanisms of cellular recognition based on Ab specificity: firstly, when the anti-HER2 mAb trastuzumab bridges target cells and cytotoxic lymphocytes armed with a Fc receptor (ADCC) and, secondly, when HER2 positive target cells are directly recognized by cytotoxic lymphocytes armed with a chimeric antigen receptor (CAR). To compare these two mechanisms, we used the same cellular effector (NK-92) and the same signaling domain (Fc ε RI γ ). The NK-92 cytotoxic cell line was transfected with either a Fc γ RIIIa-Fc ε RI γ  (NK-92 CD16 ) or a trastuzumab-based scFv-Fc ε RI γ  chimeric receptor (NK-92 CAR ). In vitro, the cytotoxic activity against HER2 positive target cells after indirect recognition by NK-92 CD16  was always inferior to that observed after direct recognition by NK-92 CAR . In contrast, and somehow unexpectedly, in vivo, adoptive transfer of NK-92 CD16  + trastuzumab but not of NK-92 CAR  induced tumor regression. Analysis of the in vivo xenogeneic system suggested that the human CH2-CH3 IgG2 used as a spacer in our construct was able to interact with the FcR present at the cell surface of the few NSG-FcR+ remaining immune cells. This interaction, leading to blockage of the NK-92 CAR  in the periphery of the engrafted tumor cells, stresses the critical role of the composition of the spacer domain.

journal of immunology research

In Vitro and In Vivo Comparison of Lymphocytes Transduced with a Human CD16 or with a Chimeric Antigen Receptor Reveals Potential Off-Target Interactions due to the IgG2 CH2-CH3 CAR-Spacer