Extended Data Fig. 7: The pro-domain of pro-IL-18 mediates the interaction with caspase-4.
From: Structural insights into cytokine cleavage by inflammatory caspase-4
a, c, Immunoblots showing in vitro cleavage of pro-IL-18 mutants by caspase-4. The pro-domain chimera consists of the pro-domain of murine pro-IL-18 fused to the mature domain of human pro-IL-18. Immunoblots are representative of three biological replicates. b, Sequence alignment of human and murine pro-IL-18. Identical and similar amino acids are highlighted in red or white boxes, respectively. Sequences were aligned using ClustalOmega online tool and plotted in ESPript 3.0. d-h, Immunoblots showing in vitro cleavage of murine pro-IL-18 mutants by caspase-4. i, ITC analysis of binding of mature IL-18 to WT caspase-4. j, Immunoblots showing in vitro cleavage of human pro-IL-18 ΔN24 by caspase-4. Pro-IL-18 ΔN24 lacks the first 24 amino acids at the N-terminus. k, Analytical SEC demonstrating no binding between pro-IL-18 ΔN24 and caspase-4. All data are representative of three independent repeats. For gel source data, see Supplementary Fig. 1.
