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An Assay for the Seeding of Homotypic Pyrin Domain Filament Transitions.

Methods in molecular biology (Clifton, N.J.)

Authors: Inga V Hochheiser, Matthias Geyer

Pattern recognition receptors of innate immune cells allow the recognition of invariant microbial structures. The nucleotide-binding oligomerization domain-like receptors (NLRs) comprise 22 members, divided into 3 subfamilies. Homotypic pyrin domain (PYD) interactions were shown to mediate the interaction of inflammasome forming NLRPs with the adaptor protein ASC, bridging the interaction to caspase-1 and resulting in caspase-1-induced cytokine maturation and pyroptotic cell death. Here we describe a NLRP3-mediated ASC polymerization assay that reconstitutes the transition from the NLRP3 nucleation seed to ASC adaptor filament elongation with recombinant proteins.

© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

PMID: 35759199

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