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Supplementary Material for:

Homodimerization attenuates the anti-inflammatory activity of interleukin-37

Andrew M. Ellisdon, Claudia A. Nold-Petry, Laura D?Andrea, Steven X. Cho, Jason C. Lao, Ina Rudloff, Devi Ngo, Camden Y. Lo, Tatiana P. Soares da Costa, Matthew A. Perugini, Paul J. Conroy, James C. Whisstock,* Marcel F. Nold*

*Corresponding author. Email: james.whisstock{at} (J.C.W.); marcel.nold{at} (M.F.N.)

Published 10 February 2017, Sci. Immunol. 2, eaaj1548 (2017)
DOI: 10.1126/sciimmunol.aaj1548

This PDF file includes:

  • Fig. S1. Structural alignment of IL-37b.
  • Fig. S2. Isoforms and sequence alignment of IL-37.
  • Fig. S3. Structural comparison of IL-37b and IL-18.
  • Fig. S4. Structural alignment of IL-37b with IL-36γ.
  • Fig. S5. The IL-37b dimer is not compatible with the classic IL-1 cytokine family binding mechanism.
  • Fig. S6. SEC of Natural46–218 and D73K46–218 at low concentration.
  • Fig. S7. Effects of transfected IL-37b variants in THP-1 cells deficient in IL-1R8.
  • Fig. S8. In vivo pharmacokinetics of IL-37b variants after intraperitoneal injection.
  • Fig. S9. Characterization of the IL-37?blocking antibody.
  • Table S1. MW determination of IL-37 and IL-18 by MALS.

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