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. 2021 Apr 12;12:2173. doi: 10.1038/s41467-021-22359-x

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© The Author(s) 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. 3 — 293T cells were transfected with plasmids encoding either wild-type or mutant FLAG-tagged KIR2DL2 and KIR2DL3 and then stained with a FLAG-specific mAb or HLA-C*03:04-GL9 and HLA-C*07:02-RL9 tetramers. Representative dot plots showing staining to cells expressing wild-type KIR2DL2 and KIR2LD3 (a). Relative binding of wild-type (WT) KIR2DL2 and KIR2DL3 transfected 293T cells and their respective alanine mutants to phycoerythrin-conjugated tetramers of HLA-C*03:04-GL9 (b) and HLA-C*07:02-RL9 (c). Transfected cells were stained for FLAG as a marker of KIR2DL expression and separately stained with HLA tetramers. Percentage tetramer+ was normalised to percentage FLAG + to account for differing KIR2DL transfection efficiency between mutants. The data represent a minimum of n = 3 independent experiments; bar line = mean, error bars = standard error of the mean (SEM); individual data points = circles (2DL2) or squares (2DL3). For each independent replicate, relative tetramer staining was normalised to staining of WT KIR2DL. Statistically significant differences in ligand recognition between corresponding mutants of KIR2DL2 and KIR2DL3 as measured by Two-way ANOVA Šidák’s multiple comparison test are highlighted. 2DL2 (n = 5) vs. 2DL3 (n = 3) binding to C*03:04-GL9 K44A: *P = 0.0127; 2DL2 (n = 5) vs. 2DL3 (n = 3) binding to C*03:04-GL9 S133A: ***P = 0.0005; 2DL2 (n = 5) vs. 2DL3 (n = 3) binding to C*07-02-GL9 D135A: ***P = 0.0007.