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Rapid Generation of Amyloid from Native Proteins In vitro
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Oxidation-sensitive cysteines drive IL-38 amyloid formation.

Alejandro Diaz-Barreiro1, Gea Cereghetti2, Francisco Gabriel Ortega Sánchez3

  • 1Division of Rheumatology, Department of Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland; Department of Pathology and Immunology, Faculty of Medicine, University of Geneva, Geneva, Switzerland; Geneva Centre for Inflammation Research, Geneva, Switzerland.

Cell Reports
|November 3, 2024
PubMed
Summary
This summary is machine-generated.

Interleukin-38 (IL-38) forms amyloid aggregates under oxidative stress, releasing from skin cells. This oxidation-induced aggregation supports epithelial barrier function.

Keywords:
CP: Molecular biologyIL-1 cytokine familyIL-38amyloid coredisulfide bridgesepidermislow complexity regionprotein aggregationredox switchunconventional secretionvicinal cysteines

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Area of Science:

  • Immunology
  • Biochemistry
  • Cell Biology

Background:

  • Interleukin (IL)-1 family cytokines are crucial for host defense at epithelial barriers.
  • IL-33, an IL-1 family member, has been linked to stress granule formation.
  • Proteins with low-complexity regions (LCRs) promote the formation of biomolecular condensates like stress granules.

Purpose of the Study:

  • To investigate the role of IL-38, an IL-1 family member, in cellular responses to oxidative stress.
  • To explore the potential for LCRs in IL-1 family members to form aggregates.
  • To understand the mechanism and function of IL-38 aggregation in keratinocytes.

Main Methods:

  • Computational analysis to predict LCRs in IL-1 family members.
  • Cellular studies observing IL-38 localization and aggregation under oxidative stress.
  • In vitro experiments to characterize IL-38 aggregation.
  • Biochemical techniques including disulfide-bond mapping and mutational analysis.
  • In silico modeling to understand conformational changes.

Main Results:

  • Computational analysis identified LCRs in six IL-1 family members, including a long LCR with amyloid cores in IL-38.
  • IL-38 was observed to form intracellular granules in keratinocytes and amyloid aggregates under oxidative stress, both in cells and in vitro.
  • Soluble and aggregated IL-38 were released from keratinocytes via an exosome-enriched extracellular vesicle fraction.
  • Oxidation-sensitive cysteines were identified as redox switches that alter IL-38 conformation and promote aggregation.
  • IL-38 granules were detected in human epidermis exposed to environmental oxidative stress.

Conclusions:

  • IL-38 possesses an intrinsic property of oxidation-induced amyloidogenesis.
  • This aggregation mechanism, involving redox switches and LCRs, plays a role in supporting epithelial barrier function.
  • IL-38's behavior suggests a novel mechanism of host defense involving stress-induced protein aggregation and release.