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. 2022 Dec 7;13:7535. doi: 10.1038/s41467-022-35071-1

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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. 3 — A Matrix heatmap representation of CD1a antibody binding by flow cytometry as measured by CD1a-AF647 mean fluorescence intensity (MFI). Before staining of CD1a-K652 with anti-CD1a antibodies conjugated to fluorophore AF647 (horizontal axis), the relevant purified antibodies (vertical axis) were incubated with the cells to assess interference in CD1a binding of the AF647-conjugated antibodies. Greyscale shows degree of binding, with the tone in the top row (−) indicating no interference. Representative of 3 independent experiments. B Matrix heatmap representation of CD1a antibody binding to CD1a mutant proteins as represented by normalized CD1a-AF647 MFI. Biotinylated CD1a mutant proteins and wild-type CD1a proteins were conjugated to streptavidin magnetic beads and binding of the panel of AF647-conjugated anti-CD1a antibodies was determined by flow cytometry. Greyscale shows degree of binding as a percentage of parent CD1a minor allele. Examined over 4 independent experiments. C Summary of CD1a mutants that affect binding of anti-CD1a antibodies OX77a, OX111, OX16, OX110. The top surface of CD1a (grey) is formed by α 1 and α 2 helices. The approximate area of A’ roof/F’ portal is marked with pink and cyan bars. The side chains of residues mutated to alanine are shown in magenta (A’ roof) or cyan (F’ portal). Mutated residues that had a negative impact on binding to the corresponding Ab are labelled and their surface is coloured in red.