RESEARCH HIGHLIGHT - The structural differences between patient-derived α-synuclein strains dictate characteristics of Parkinson’s disease, multiple system atrophy and dementia with Lewy bodies

In this Acta Neuropathologica publication, IMPRIND Partner CNRS establishes a method where seeds from frozen brain tissues can seed the aggregation of pure alpha-synuclein (α-syn). This allowed demonstrating that the resulting aggregates possess distinct biochemical properties in vitro and pathological properties in an animal model. The fibrils obtained by amplification of pathogenic α-syn from different PD cases exhibit identical structural properties. The same is true for fibrils obtained from DLB and MSA cases. Comparison of fibrils derived from PD, MSA and PD cases shows they exhibit distinct biochemically and pathological properties. 

Thus, each synucleinopathy appears to differ from others by the biochemical and pathological properties of the fibrils.

This project receives funding from the Innovative Medicines Initiative 2 Joint Undertaking ( under grant agreement No 116060. This Joint Undertaking receives support from the European Union’s Horizon 2020 research and innovation programme and EFPIA.

This work is supported by the Swiss State Secretariat for Education‚ Research and Innovation (SERI) under contract number 17.00038.

The opinions expressed and arguments employed herein do not necessarily reflect the official views of these funding bodies.

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