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Fig. S1. The Nacht leucine rich repeat and pyrin domain containing protein 3 (NALP3) inflammasome activates interleukin (IL)-1β and IL-18. NALP3 has three domains: an N-terminal protein–protein interaction domain, called PYD; a central nucleotide-binding and oligomerization domain, called NACHT; and a C-terminal ligand-binding and regulatory leucin-rich repeat domain, called LRR. NACHT is encoded by exon 3. PYD interacts with a protein called ASC, which stands for ‘apoptosis-associated speck-like protein containing a caspase recruitment domain’ (CARD). This interaction then binds pro-caspase-1 to ASC via homodimerization of the respective CARD domains. This is called the NALP3 inflammasome. Upon activation by ligand binding [e.g. adenosine triphosphate (ATP)] to the LRR of NALP3 caspase-1 dimerizes, resulting in proximity-induced autoactivation. Active, p10/20-tetrameric caspase-1 is released from the complex to cleave IL-1β and IL-18 precursors into their active forms.

Fig. S2. Subdivision of patients. Flowchart of the individuals studied per experiment. Patients per group: ●; patients per group with duration of treatment in months: image; patient numbers from Table 1: #; patients with Anakinra added to their peripheral blood mononuclear cells (PBMCs) in vitro or treated with Anakinra in vivo: V. Patients per group with duration of treatment in months per dose of Rilonacept image.

Fig. S3. Diagram explaining low stimulation indices (SIs) in neonatal-onset multi-system inflammatory disease (NOMID) patients with improvement of SIs by Anakinra therapy in vitro but not in vivo.

Table S1. Raw data for Fig. 2a. Interleukin (IL)-1β production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S2. Raw data for Fig. 2b. Interleukin (IL)-6 (pg/ml) production after stimulation with phytohaemagglutinin (PHA).

Table S3. Raw data for Fig. 2c. Interleukin (IL)-10 (pg/ml) production after stimulation with phytohaemagglutinin (PHA).

Table S4. Raw data for Fig. 2d. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S5. Raw data for Fig. 2e. Interleukin (IL)-12p70 production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S6. Raw data for Fig. 2f. Interferon (IFN)-γ production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S7. Raw data for Fig. 2g. Interferon (IFN)-γ production (pg/ml) after stimulation with phytohaemagglutinin (PHA)+interleukin (IL)-12.

Table S8. Raw data for Fig. 3a. Interleukin (IL)-1β (pg/ml) production after stimulation with lipopolysaccharide (LPS).

Table S9. Raw data for Fig. 3b. Interleukin (IL)-6 production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S10. Raw data for Fig. 3c. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S11. Raw data for Fig. 3d. Interleukin (IL)-12p70 production (pg/ml) after stimulation with LPS.

Table S12. Raw data for Fig. 3e. Interleukin (IL)-1β (pg/ml) production after stimulation with lipopolysaccharide (LPS)+interferon (IFN)-γ.

Table S13. Raw data for Fig. 3f. Interleukin (IL)-6 production (pg/ml) after stimulation with lipopolysaccharide (LPS)+interferon (IFN)-γ.

Table S14. Raw data for Fig. 3g. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with lipopolysaccharide (LPS)+interferon (IFN)-γ.

Table S15. Raw data for Fig. 3h. Interleukin (IL)-12p70 production (pg/ml) after stimulation with lipopolysaccharide (LPS)+interferon (IFN)-γ.

Table S16. Raw data for Fig. 4a. Interleukin (IL)-1β (pg/ml) production after stimulation with phytohaemagglutinin (PHA).

Table S17. Raw data for Fig. 4b. Interleukin (IL)-6 production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S18. Raw data for Fig. 4c. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S19. Raw data for Fig. 4d. Interferon (IFN)-γ production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S20. Raw data for Fig. 4e. Interleukin (IL)-1β (pg/ml) production after stimulation with lipopolysaccharide (LPS).

Table S21. Raw data for Fig. 4Ff. Interleukin (IL)-6 production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S22. Raw data for Fig. 4g. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S23. Raw data for Fig. 4h. Interferon (IFN)-γ production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S24. Raw data for Fig. 5a. Interleukin (IL)-1β production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S25. Raw data for Fig. 5b. Interleukin (IL)-6 production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S26. Raw data for Fig. 5c. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S27. Raw data for Fig. 5d. Interferon (IFN)-γ production (pg/ml) after stimulation with phytohaemagglutinin (PHA).

Table S28. Raw data for Fig. 5e. Interleukin (IL)-1β (pg/ml) production after stimulation with lipopolysaccharide (LPS).

Table S29. Raw data for Fig. 5f. IL-6 production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S30. Raw data for Fig. 5g. Tumour necrosis factor (TNF) production (pg/ml) after stimulation with lipopolysaccharide (LPS).

Table S31. Raw data for Fig. 5h. Interferon (IFN)-γ production (pg/ml) after stimulation with lipopolysaccharide (LPS).

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