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NLRP12 interacts with NLRP3 to block the activation of the human NLRP3 inflammasome

This work describes a new role for the NLRP12 protein. We found that human NLRP12 does not form an inflammasome but instead regulates NLRP3 activation. The work shows that although the PYD domain of NLRP12 can bind ASC, its NACHT domain cannot oligomerise. Our data is also supported by NLRP12 mutations present in patients who display hyperactivation of NLRP3. 

Extracorporeal Membrane Oxygenation–Dependent Fulminant Melioidosis From Caspase 4 Mutation Reversed by Interferon Gamma Therapy. 

First identification of a mutation in Caspase-4 in human. The mutation identify render the individual susceptible to bacterial infections, identifying a novel immunopathology driven by the non-canonical inflammasome. The mutation unveils novel information about caspase-4 biochemistry and its role in human infections

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Caspase-4 dimerisation and D289 auto-processing elicits an interleukin-1β converting enzyme

We unveil the mechanism controlling caspase-4 activation. We also identify a novel substrates for caspase-4, interleukine 1B, and characterise the mechanism controlling it.

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Inflammatory caspases: toward a unified model for caspase activation by inflammasomes

Here, we review the mechanisms that control inflammatory caspases activation and activity, summarising our (and others) research effort to better understand these critical inflammatory enzymes

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Access the Boucher lab publications here

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