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. 2017 Sep 6;7:10713. doi: 10.1038/s41598-017-11126-y

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© The Author(s) 2017

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Design of the TCR-CAR constructs. (a) TCR-CAR gene design was based on the strategy previously used to produce soluble TCR (sTCR) in mammalian cells²⁴: TCRα and β chain were truncated at the level of their TM region, cysteines were added on their constant domains and the two chains were linked by a 2A peptide sequence. The artificial STOP codon of the TCRβ chain sTCR was replaced by the transmembrane (TM) domain of CD28 followed by a second generation CAR signalling tail composed of CD28 and CD3ζ signalling domains. The expected product of the TCR-CAR coding sequence should be two separated proteins released in the ER at equimolar amounts. (b) sTCR was produce as a soluble protein which, probably following the vesicular secretion pathway, was released in the cellular medium (left). TCR-CAR is expected to be exported to the cell surface as an TCRα/β heterodimer. Correct folding should ensure specific binding to a peptide-MHC (pMHC) complex and signal transduction through CD28-CD3 signalling tail (right).