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. 2022 Aug 16;13:4822. doi: 10.1038/s41467-022-32401-1

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© The Author(s) 2022

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 Analysis of STING dimerization in WT and IRF8-KO THP-1 cells infected with HSV-1 for the indicated times. The lysates were fractionated by non-reducing SDS-PAGE or SDS-PAGE and analyzed with the indicated antibodies. b Analysis of Sting polymerization in WT and Irf8^−/− BMDMs infected with HSV-1 for the indicated times. The lysates were fractionated by Blue Native PAGE or SDS-PAGE and analyzed by immunoblots with the indicated antibodies. c Gel filtration chromatography in WT and Irf8^−/− BMDMs. BMDMs were left uninfected and infected with HSV-1 for 4 h before lysis. The individual fractions were analyzed by immunoblotting with the indicated antibodies. Fraction sizes were calibrated with the gel filtration standard (Bio-Rad 151-1901). d Endogenous association of Sting with Tbk1 and Irf3 in WT and Irf8^−/− BMDMs. The cells were left uninfected or infected with HSV-1 for the indicated times. Co-immunoprecipitation and immunoblotting analysis were performed with the indicated antibodies. Source data are provided as a Source data file.