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. 2023 May 9;14:2463. doi: 10.1038/s41467-023-37863-5

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© The Author(s) 2023

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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Fig. 1 — a A benzylguanine motif (BG) is chemically conjugated to an antibody using a benzylguanine NHS ester. The BG-antibody conjugate then covalently binds to the extracellular SNAPtag enzyme through a self-labeling reaction. b SNAPtag receptors enable the targeting of multiple different antigens using the same receptor by combining SNAP receptor cells with different BG-conjugated antibodies. c The SNAP-synNotch receptor is targeted by a BG-conjugated antibody and upon antigen recognition leads to cleavage of the synNotch receptor, releasing the transcription factor and transcriptional regulation of a target gene or genes. d The SNAP-CAR is targeted by a BG-conjugated antibody to activate T cell signaling and effector functions upon antigen recognition.