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NALP3 inflammasome activation by prion protein fibrils
Hafner Bratkovič, Iva, 1978- ...
Transmissible spongiform encephalopathies (prion diseases) are characterized by accumulation of abnormal form of prion protein, spongiform change, gliosis and progressive neuronal cell loss; however, ...the underlying cause of neurodegeneration is not known. Previous studies have indicated the role of innate immunity, particularly of Nalp3 inflammasome in other amyloid diseases - Alzheimer's disease and type 2 diabetes. Production of proinflammatory cytokine IL-1[beta] has also been observed in brain in several types of prion disease and IL-1R deficiency significantly prolonged the onset of the disease. The aim of ourstudy was to investigate whether prion protein assemblies can instigate Nalp3 inflammasome. We prepared several types of assemblies of prion protein and biophysically characterized them. We show that PrP fibrils, converted from [alpha]- to predominantly [beta] -type conformation trigger clevage of pro-IL-1[beta], which requires the inflammasome components Nalp3, ASC and caspase-1, whereas the native cellular form of prion protein does not induce activation of IL-1[beta]. Several of the previously proposed Nalp3 inflammasome activation pathways may contribute to prion fibril induced inflammasome activation, since it can be blocked by ROS inhibitors, inhibition of K+ efflux and inhibition of phagocytosis. Proteinase K resistant PrP fibrils, but not monomers, induce release of neurotoxic species by microglial cells and can thus contribute to neuronal cell death.
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