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. 2016 Dec 1;4:126. doi: 10.1186/s40478-016-0397-1

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 8 — Comparison of antibody binding to four full-length D2R mutants. Binding was similar between N23Q and N23Q/D26E/A29P mutants with WT D2R (100% binding shown as dotted line). Murinization of amino acids 26 and 29 (D26E/A29P) strongly reduced binding. Interestingly, L R20K/P21G/F22W/N23Q/D26E/A29P mutant had the greatest impact on antibody binding. Percentage of sera binding to D2R mutants (MFI %) was calculated using the formula described in Material and Methods. Results are expressed as mean ± SD %. Data was analyzed by one-way ANOVA analysis of variants with a Dunn’s multiple comparison test, *P < 0.05, **P < 0.01, ***P < 0.001