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. 2021 May 3;14:75. doi: 10.1186/s13045-021-01084-4

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© The Author(s) 2021

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 — Structures of bispecific T cell-recruiting antibodies. A bispecific T cell engager (BiTE) consists of two single-chain variable fragments (scFvs); a dual-affinity retargeting antibody (DART) consists of two engineered scFvs whose V_H exchanged with the other one; a TandAb consists of two single-chain diabodies with four variable domains; a XmAb consists of one scFv, one Fab fragment and one hetero-Fc domain; a 2:1 Crossmab contains two tumor antigen binders and one CD3 binder; “knob in hole” technique and duobody technique enable production of bispecific antibodies with similar structures to natural IgG