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. 2023 Jan 4;14:61. doi: 10.1038/s41467-022-35725-0

Fig. 6. Biochemical and functional characterization of the interactions between GSDMD and IpaH7.8.

Fig. 6

a Quantification of the binding affinity between human GSDMD (hGSDMD) and IpaH7.8 by ITC. b In vitro pull-down of WT or mutant hGSDMD proteins by His-tagged IpaH7.8. c IpaH7.8 triggered the hGDSMD degradation. Cellular degradation assays in cells expressing the IpaH7.8 and hGSDMD proteins indicated. C357S, IpaH7.8 catalytic dead mutant. insR20, insertion of an additional arginine after the 19th residue. Cells were treated with or without MG132. d Structural alignments of NTD-GSDMB with human and mouse NTD-GSDMD. mGSDMD, mouse GSDMD. e Sequence alignment of the α1-α2 loop regions across the GSDMs. Invariant residues are shaded red. f IpaH7.8 induced the degradation of GDSMB. insR20, insertion of an additional arginine after the 19th residue. Cells were treated with or without MG132. g Cellular degradation assays showing that mouse GSDMD (mGSDMD) could be susceptible to IpaH7.8-mediated degradation when mutating both the 17th and 20th residues. Cells were treated with or without MG132. Source data are provided as a Source Data file.