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. 2021 Feb 8;5(5):455–466. doi: 10.1038/s41551-020-00675-9

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© The Author(s), under exclusive licence to Springer Nature Limited 2021, corrected publication 2021

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. 4 — a, Schematic of site-directed mutagenesis on the STING structure. Mutation sites are distinct from the cGAMP-binding pocket. b,c, STING mutation of E296A/D297A abolishes STING condensation (b) and immune activation (c) in response to PC7A. Other mutations in STING do not affect PC7A-induced STING activation. Data are mean ± s.d. n = 3 biologically independent experiments. Statistical analysis was performed using one-way ANOVA. d–f, PC7A retains immune activity in several cGAMP-resistant STING variants. R232H in THP1 cells (d) or R238A/Y240A in HeLa cells (f) abrogates cGAMP binding. Q273A/A277Q (e,f), which disrupts the tetramer interface and cGAMP-mediated STING oligomerization, abolishes STING activation by cGAMP but not by PC7A. Data are mean ± s.d. n = 3 biologically independent experiments. Statistical analysis was performed using two-tailed Student’s t-tests. c, cGAMP; m, mock; p, PC7A polymer.