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. 2020 May 18;10:8177. doi: 10.1038/s41598-020-64847-y

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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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Tat specifically bind to TLR4/MD2. (A) Characterization of GST-Tat binding to recombinant TLR4/MD2 (Coating 1 µg/ml) by ELISA. GST was used as control. The data represent means and SD for three independent experiments. Statistical significance was analyzed by one-way ANOVA follow by Bonferroni post tests and is marked as follows: *P < 0.05; **P < 0.01; ***P < 0.001; ns, non significant. (B) Cell surface binding assay: HEK (Null) or HEK TLR4-CD14-MD2 were incubated with GST-Tat1-101 or GST alone for 60 min at 4 °C. Cells were stained with anti-GST and anti-TLR4 antibodies or the corresponding isotypic control antibodies. Secondary antibodies conjugated with Alexa Fluor-555 and Alexa Fluor-488 were used to detect anti-GST and anti-TLR4 antibodies respectively. Cells nuclei were stained with DAPI. Cells were imaged using confocal Zeiss LSM 710 (Image Core facility, CPTP, Toulouse) using a 63x objective. Colocalization and subcellular localization were analyzed and processed with ImageJ software.