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. 2020 May 26;11:2623. doi: 10.1038/s41467-020-16397-0

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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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Fig. 2 — a A prominent hydrophobic interaction. Phe476 of VpdB packs against a hydrophobic pocket on LvgA indicated by the dotted line. Four residues that constitute the hydrophobic pocket are shown as sticks. b Native PAGE analysis. The VpdB(F476E) or LvgA(I153E) mutation disrupted the interaction between VpdB(11-590) and (His)₁₀-MBP-DotL(656-783)–IcmSW–LvgA. c Quantification. The binding affinity between (His)₁₀-MBP-DotL(656-783)–IcmSW–LvgA and VpdB(11-590) was drastically decreased by either VpdB(F476E) or LvgA(I153E) mutation. The interaction was measured by bio-layer interferometry, where the indicated bait was immobilized on a Ni-NTA biosensor via the N-terminal (His)₁₀-MBP tag fused to DotL(656-783). The measurement was triplicated. d Alanine mutagenesis. Binding affinities between (His)₁₀-MBP-DotL(656-783)–IcmSW–LvgA and VpdB(11-590) variants containing the indicated alanine substitution were analyzed by bio-layer interferometry. A plot of the measured K_D values is shown on the right. Quantification was duplicated for each variant.