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Updated: May 28, 2025

Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells
Published on: May 22, 2014
Mechanisms of NLRP3 activation and inhibition elucidated by functional analysis of disease-associated variants
Shouya Feng1,2,3,4, Matthew C Wierzbowski3,4,5, Katja Hrovat-Schaale3,4
1Centre for Innate Immunity and Infectious Diseases, Hudson Institute of Medical Research, Clayton, Victoria, Australia.
Abstract:
The NLRP3 inflammasome is a multiprotein complex that mediates caspase-1 activation and the release of proinflammatory cytokines, including interleukin (IL)-1β and IL-18. Gain-of-function variants in the gene encoding NLRP3 (also called cryopyrin) lead to constitutive inflammasome activation and excessive IL-1β production in cryopyrin-associated periodic syndromes (CAPS). Here we present functional screening and automated analysis of 534 NLRP3 variants from the international INFEVERS registry and the ClinVar database. This resource captures the effect of NLRP3 variants on ASC speck formation spontaneously, at low temperature, after inflammasome stimulation and with the specific NLRP3 inhibitor MCC950. Most notably, our analysis facilitated the updated classification of NLRP3 variants in INFEVERS. Structural analysis suggested multiple mechanisms by which CAPS variants activate NLRP3, including enhanced ATP binding, stabilizing the active NLRP3 conformation, destabilizing the inactive NLRP3 complex and promoting oligomerization of the pyrin domain. Furthermore, we identified pathogenic variants that can hypersensitize the activation of NLRP3 in response to nigericin and cold temperature exposure. We also found that most CAPS-related NLRP3 variants can be inhibited by MCC950; however, NLRP3 variants with changes to proline affecting helices near the inhibitor binding site are resistant to MCC950, as are variants in the pyrin domain, which likely trigger activation directly with the pyrin domain of ASC. Our findings could help stratify the CAPS population for NLRP3 inhibitor clinical trials and our automated methodologies can be implemented for molecules with a different mechanism of activation and in laboratories worldwide that are interested in adding new functionally validated NLRP3 variants to the resource. Overall, our study provides improved diagnosis for patients with CAPS, mechanistic insight into the activation of NLRP3 and stratification of patients for the future application of targeted therapeutics.
Insights
This study functionally screened 534 NLRP3 variants, revealing mechanisms of cryopyrin-associated periodic syndromes (CAPS) and identifying variants responsive to MCC950 inhibition. Findings aid CAPS diagnosis and patient stratification for targeted NLRP3 inhibitor therapies.
Area of Science:
- Immunology
- Genetics
- Molecular Biology
Background:
- The NLRP3 inflammasome, crucial for immune responses, is implicated in cryopyrin-associated periodic syndromes (CAPS) due to gain-of-function variants.
- Constitutive inflammasome activation by these variants leads to excessive IL-1β production, driving CAPS pathogenesis.
Purpose of the Study:
- To functionally screen a large set of NLRP3 variants and elucidate their impact on inflammasome activation.
- To update the classification of NLRP3 variants and understand mechanisms of CAPS pathogenesis.
- To identify patient subgroups responsive to NLRP3 inhibitors like MCC950.
Main Methods:
- Functional screening and automated analysis of 534 NLRP3 variants from INFEVERS and ClinVar databases.
- Assessment of ASC speck formation under various conditions (spontaneous, cold, stimulation, MCC950 treatment).
- Structural analysis to determine variant-specific activation mechanisms.
Main Results:
- Updated classification of NLRP3 variants, with identified mechanisms including enhanced ATP binding and altered NLRP3 conformation.
- Discovery of variants hypersensitizing NLRP3 activation to nigericin and cold.
- Most CAPS variants are MCC950-inhibitable, but resistance is observed in variants near the binding site or in the pyrin domain.
Conclusions:
- Provides mechanistic insights into NLRP3 activation and CAPS.
- Facilitates improved diagnosis and stratification of CAPS patients for targeted NLRP3 inhibitor therapies.
- Offers a scalable methodology for functional variant characterization.
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