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. 2020 Jun 29;10:10522. doi: 10.1038/s41598-020-67468-7

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© The Author(s) 2020

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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Luciferase reporters provide highly sensitive detection of the Cd200-Cd200R interaction. Highly avid rat Cd200 prey proteins containing the reporter enzymes (a) beta-lactamase (BLac), (b) Gaussia luciferase (GLuc) or (c) nano-luciferase (NanoLuc) were probed for interactions with a biotinylated rat Cd200R bait protein immobilised in streptavidin-coated microtitre plates. Prey capture was quantified using absorbance at 485 nm for hydrolysis products of the beta-lactamase colourimetric substrate nitrocefin, and luminescence using the substrates coelenterazine (Gaussia luciferase) and furimazine (nano-luciferase). Cd200 was used as a negative control bait (empty circles). The normalised signal for each data point was calculated as described in the Methods such that background signal would be 0 and the maximum signal 1. The log IC50 for each interpolated curve is displayed on each graph. Representative experiments shown with n = 3 for each concentration of prey with s.e.m. for each data point and the 95% CI for the interpolated curves indicated as dotted lines.