Abstract
Aggregates of α-synuclein protein can form in various cell types and cause different neurodegenerative disorders. The existence of strains with distinct structural conformations might explain this variability. See Letter p.340 Synucleinopathies are neurodegenerative disorders characterized by α-synuclein-rich protein deposits which include Parkinson's disease, dementia with Lewy bodies and multiple system atrophy. The discovery of α-synuclein assemblies with different structural characteristics has led to the hypothesis that different 'strains' could account for pathological differences between these different neurodegenerative diseases. This study reports that when different human α-synuclein strains — oligomers, ribbons or fibrils — are injected into rat brain in vivo, they propagate in a strain-dependent manner and cause different pathological and neurotoxic phenotypes. This work has implications for disease diagnosis and prognosis and for the prospects of developing therapeutic strategies tailored for specific synucleinopathies.
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