Fig. 4: Characterization of the interactions between TcsH and TMPRSS2 by structure-based mutagenesis. | Nature Communications

Fig. 4: Characterization of the interactions between TcsH and TMPRSS2 by structure-based mutagenesis.

From: Molecular basis of TMPRSS2 recognition by Paeniclostridium sordellii hemorrhagic toxin

Fig. 4: Characterization of the interactions between TcsH and TMPRSS2 by structure-based mutagenesis.

a Binding of the wild-type TcsH2210-2618 to Fc-His-TMPRSS2ECD variants immobilized on Protein A resins was examined using pull-down assays. b The binding of TcsH2210-2618 variants to Fc-His-TMPRSS2ECD immobilized on Protein A resins was examined using pull-down assays. c Confocal fluorescence images show the binding of different GFP-fused TcsH2210-2618 variants to the MCF-7 GMDS‒/‒ cells. Cell nuclei were stained by DAPI (blue). The blots and images are representatives of three independent experiments. The scale bar represents 50 μm. d, e The sensitivities of the MCF-7 GMDS‒/‒ and TMPRSS2‒/‒ cells to TcsH or its mutants were tested using the cytopathic cell-rounding assays. The percentages of the rounded cells were plotted over the toxin concentrations. Error bars (n = 5 biologically independent samples) indicate mean ± SD. Source data are provided as a Source Data file.

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