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. 2020 May 5;39:77. doi: 10.1186/s13046-020-01572-4

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — Illustrative representation of the UniCAR system and the αSTn-IgG4 TM construct. a The UniCAR system can be combined with different TM formats, namely scFv- and IgG4-based TMs, to specifically redirect UniCAR T-cells to tumor cells via the E5B9 epitope. UniCAR T-cells are genetically engineered to express the humanized scFv derived from the anti-La mAb 5B9 fused to the transmembrane domain of human CD28 and intracellular signaling domains of CD28 and CD3ζ. b Detailed representation of the αSTn-IgG4 TM construct, comprising the anti-STn scFv (L2A5) arranged in V_H - V_L orientation linked by a (G₄S)₃ peptide, the hinge and Fc region of the human IgG4 molecule, and the E5B9 epitope. After expression the αSTn-IgG4 TM will form homodimers due to formation of disulfide bridges between the cysteine residues present in the IgG4 hinge region. c In order to confirm UniCAR expression, genetically modified T-cells were stained with isotype control (upper panel) or anti-La mAb 7B6 (lower panel). Specific binding was detected using a PE-labeled anti-mouse-IgG mAb. Density plots show percentage of CAR surface expression (E7B6) versus expression of co-translated EGFP protein marker for one representative donor. G, glycine; S, serine; A, alanine; P, proline; C, cysteine