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A de novo dominant-negative PSMB8 mutation causes severe CANDLE/PRAAS due to arrested proteasome biogenesis

  • Sophie Wolfgramm
  • , Sara Alehashemi
  • , Martin Wendlandt
  • , Franziska G. Thiel
  • , Adriana A. de Jesus
  • , Jonas J. Papendorf
  • , Hannes Wolfgramm
  • , Flavia Llorente Alvarez
  • , Emely Borngräber
  • , Kat Uss
  • , Farzana Bhuyan
  • , Anvitha Metpally
  • , Leif Steil
  • , Christian Hentschker
  • , Simone Venz
  • , Ruba Al Abdulla
  • , L. Poirier
  • , Christopher Friend
  • , Fabiola Castello Casta
  • , Iren Horkayne-Szakaly
  • Shoghik Akoghlanian, Peter J. Mustillo, Roshini S. Abraham, Paul Bastard, Thais C. L. Moura, Mayra B. Dorna, Katia T. Kozu, Jesper Kers, Y. K. Onno Teng, Robbert G. M. Bredius, Karin Palmblad, AnnaCarin Horne, Petter Brodin, Pilar Blanco-Lobo, José Bernabeu-Wittel, Laura Fernandez-Silveira, Olaf Neth, Anne Pagnier, Guilaine Boursier, Maud Tusseau, Thomas W. J. Huizinga, Benjamin Fournier, B. nédicte Neven, Uwe Völker, Gijs W. E. Santen, Jason M. Brenchley, Katherine R. Calvo, David Kleiner, Frédéric Ebstein, Elke Krüger*, Raphaela Goldbach-Mansky*
*Corresponding author for this work
  • University of Greifswald
  • National Institutes of Health
  • L'institut du Thorax
  • Joint Pathology Center
  • Nationwide Children’s Hospital
  • Université Paris Cité
  • Rockefeller University
  • Universidade de São Paulo
  • Leiden University
  • Erasmus University Rotterdam
  • Amsterdam UMC - University of Amsterdam
  • Karolinska Institutet
  • Hospital Universitario Virgen del Rocio
  • Université Grenoble Alpes
  • Cellules Souches, Plasticité Cellulaire, Régénération Tissulaire et Immunothérapie des Maladies Inflammatoires
  • Hospices civils de Lyon

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Abstract

Objectives: Proteasome-associated autoinflammatory syndromes (PRAAS) include a group of autoinflammatory interferonopathies caused by 20S proteasome dysfunction. We characterised pathomechanisms and treatment responses of patients with a de novo, dominant-negative (DN)-proteasome subunit beta type-8 (PSMB8) variant. Methods: Patients with the DN-PSMB8 p.G209R variant encoding a mutant β5i subunit of the 20S immunoproteasome were evaluated. Interferon biomarkers, proteasome activity, structural modelling, and proteotoxic stress responses were assessed. Patients’ T cells underwent integrated transcriptomic and proteomic profiling to characterise immune dysregulation, proteotoxic stress responses, mitochondrial function, and type I interferon (IFN-I) associated stress signalling. Results: Patients with DN-PRAAS presented with early-onset systemic inflammation, panniculitis, cytopenias, infections, and porto-sinusoidal vascular liver disease (PSVD), indicating broader immune dysfunction that partially responds to Janus kinase inhibition and/or interferon-α/β receptor blockade (anifrolumab). Mechanistically, the PSMB8 p.G209R variant caused steric hindrance that impaired β5i propeptide processing and final 20S proteasome formation, resulting in intracellular protein aggregation, impaired mitochondrial metabolism, and altered neutral lipid processing. The IFN-I signature of patients’ T cells was reduced by blockade of 2 integrated stress response (ISR)-regulating kinases, protein kinase R (PKR) and general control nonderepressible 2 (GCN2), and by Janus kinase signalling. Conclusions: The DN-PSMB8 p.G209R variant broadens the clinical and mechanistic PRAAS spectrum by causing 20S proteasome maturation arrest and uncovering a convergence between mitochondrial dysfunction and the ISR. Our findings implicate cytopenia in a pattern of vascular pathology, including PSVD of the liver. We further identify PKR and GCN2 as key mediators of maladaptive IFN-I responses and potential therapeutic targets.
Original languageEnglish
JournalAnnals of the rheumatic diseases
Early online date2025
DOIs
Publication statusE-pub ahead of print - 2025

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