Abstract
The NLRP3 and NLRP12 inflammasome complexes are a subset of the Nod‐like receptor family, known to play a key role in the innate immune system. They act by activating caspase‐1 in response to pathogens, as well as endogenous and environmental stimuli. The NLRP3 inflammasome consists of the sensing protein, NLRP3, adaptor protein ASC, and pro‐caspase‐1. The proposed structure of the complex is based on the effector domains on the proteins, although the assembly of the active complex remains unclear. Even less is known about the NLRP12 inflammasome.We used a combination of Leishmania tarentolae cell‐free expression system, AlphaScreen, and single molecule fluorescence spectroscopy to investigate the assembly of NLRP3 and NLRP12 inflammasomes. Our results suggest that the NLRP3 and NLRP12 inflammasomes have different mechanisms of assembly. We observed NLRP3 and NLRP12 forming oligomers of distinct size. While NLRP3 can bind to ASC and pro‐caspase‐1 independently, association of NLRP12 with pro‐caspase‐1 requires ASC. Interestingly, we observed that aggregation of ASC is concentration dependent and nucleation of ASC has characteristics of the seeding model proposed for prions.Grant Funding Source: Australian Research Council
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