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. 2017 Jul 19;7:5860. doi: 10.1038/s41598-017-06289-7

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© The Author(s) 2017

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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Characterization of the interaction between Ethr and c-di-GMP. (a). c-di-GMP binds protein Ethr on the protein microarray. Cy3 signal was measured at 532 nm by a fluorescence microarray scanner. +: in the presence of biotin-c-di-GMP; −: in the presence of biotin alone. (b). UV cross-linking assay for validation the interaction between Ethr and c-di-GMP. Purified GST tag Ethr was co-incubated with 1, 5, 25 μM biotinylated c-di-GMP or 25 μM biotinylated cGMP or 25 μM biotinylated c-di-GMP (Bio-c-di-GMP) with 1000 μM c-di-GMP competition. The input was visualized by a GST antibody. The relative signal to control is presented below. (c). Measure the binding kinetics of c-di-GMP and Ethr by Bio-Layer interference (BLI). Bio-c-di-GMP was immobilized on streptavidin coated biosenser and incubated with serially diluted Ethr. The measurement and calculation were carried out according to the manufacturer’s instruction.