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. 2022 Oct 25;15:153. doi: 10.1186/s13045-022-01364-7

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© The Author(s) 2022

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. 2 — Structures, distributions, interactions and biological functions of B7-H3 and putative receptors. Three proteins have been identified as potential B7-H3 receptors, including TLT-2 (A), IL20RA (B) and PLA2R1 (C). TLT-2 is widely expressed on the surface of myeloid, B and T cells, and its function in specific cell types has been separately studied. TLT-2 plays a proinflammatory role in CD8+ T cells, neutrophils and microglia while reducing the Th1 immune response and blocking Th1 differentiation when activated on monocytes. The effect of B7-H3 binding to TLT-2 on CD8+ T cells is controversial, and the functional interaction between B7-H3 and TLT-2 in other cell types remains unknown (A). Little is known about the specific cell types that express IL20RA and PLA2R1 and their cell type-specific functions. IL20RA activation enhances breast cancer cell stemness and establishes an immunosuppressive TME via the JAK1/STAT3 signaling pathway, while modulation of the TME via the JAK1/STAT3 pathway through IL20RA and IL20RB is still disputed, requiring more robust and direct evidence (B). PLA2R1 has been indicated as a tumor-suppressive regulator that induces breast cancer cell apoptosis and inhibits transformation to renal cell carcinoma (C). Considering the diverse roles of B7-H3 in the TME, other unknown receptors must be reported continuously. Human B7-H3 gene locates in 15q24.1 and has 12 exons encoding 316 amino acids; the structure of B7-H3 (4IgB7-H3 here, the major isoform in humanity) comprises two identical pairs of extracellular lgV-like and IgC-like domains, a transmembrane region and a 45-aa cytoplasmic tail. Seven B7-H family members (B7-H1 to B7-H7) and their receptors expressed on T cells are also displayed, where B7-H3 binds to TLT-2, IL20RA, PLA2R1 and other interesting as yet unknown receptors. “+” in green indicates the immunostimulatory (positive) signal, and “−” in red indicates the immunosuppressive (negative) signal (D). TME, tumor microenvironment