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. 2019 Jul 19;10:3192. doi: 10.1038/s41467-019-11173-1

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© The Author(s) 2019

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. 2 — HBx binds endogenous Bcl-xL through the BH3-like domain. a HBx-aa113–135 interacts with Bcl-xL in HepG2 cell lysate. Co-precipitation experiments were performed in the HepG2 cell lysate using biotinylated HBx-aa113–135 peptides (wild type (WT)) and corresponding mutant peptides (W120A/L123A), respectively. The results were analyzed by immunoblotting (IB) using anti-Bcl-xL antibody. β-Tubulin was measured and analyzed as an input control. b Full-length HBx interacts with Bcl-xL in HepG2 cells. Co-immunoprecipitation (co-IP) experiments were performed in HepG2 cells transfected with pTT22m-HBx-WT or pTT22m-HBx(W120A/L123A). The cell lysate was precipitated by an anti-HBx antibody and analyzed by immunoblotting using an anti-Bcl-xL antibody. c Isothermal titration calorimetry (ITC) result shows the dissociation constant between HBx113-135 and Bcl-xL is 26.5 ± 13.7 μM. d The interaction between HBx-aa113–135(W120A/L123A) and Bcl-xL is non-detectable by ITC. Source data are provided as a Source Data file