C4b-Binding Protein Inhibits Particulate- and Crystalline-Induced NLRP3 Inflammasome Activation

Authors

Damien Bierschenk
Nikolina Papac-Milicevic
Ian P Bresch
Valentina Kovacic
Serena Bettoni
Mateusz Dziedzic
Rick A Wetsel
Susanne Eschenburg
Christoph J Binder
Anna M Blom
Ben C King

Publication Date

1-1-2023

Journal

Frontiers in Immunology

Abstract

Dysregulated NLRP3 inflammasome activation drives a wide variety of diseases, while endogenous inhibition of this pathway is poorly characterised. The serum protein C4b-binding protein (C4BP) is a well-established inhibitor of complement with emerging functions as an endogenously expressed inhibitor of the NLRP3 inflammasome signalling pathway. Here, we identified that C4BP purified from human plasma is an inhibitor of crystalline- (monosodium urate, MSU) and particulate-induced (silica) NLRP3 inflammasome activation. Using a C4BP mutant panel, we identified that C4BP bound these particles

Keywords

Animals, Humans, Mice, Complement C4b-Binding Protein, Inflammasomes, Macrophages, NLR Family, Pyrin Domain-Containing 3 Protein, Silicon Dioxide

Comments

Associated Data

PMID: 37283747