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. 2019 Jul 4;10:2961. doi: 10.1038/s41467-019-10766-0

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© The Author(s) 2019

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. 6 — FHR1 binds to MDA-LDL on necrotic cells. a FHR1 binds to MDA-LDL, but not to LDL or BSA. b FHR1 binds to MDA-LDL in a dose-dependent manner as shown by ELISA and c surface plasmon resonance. d FHR1 binds to MDA epitopes on necrotic cells, as demonstrated by proximity ligation assay. Red dots denote FHR1-MDA complexes. DNA is stained with DAPI (blue). Control = one antibody. e FHR1 binds with its N-terminus FHR1 SCR1-2 to MDA-LDL. f FHR1 bound to MDA-LDL, but not LDL, increases IL-1β release by monocytes. Data in a–f represent the mean ± SEM. of three to four independent experiments with different cell donors. *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001 (unpaired two-tailed t-test)