α-Synuclein purification significantly impacts seed amplification assay performance and consistency
α-Synuclein seed amplification assays are a promising diagnostic tool for synucleinopathies such as Parkinson's disease and multiple system atrophy. Standardized conditions are required to ensure a high degree of inter- and intra-laboratory reproducibility when performing these assays. A significant issue that hinders the utility of seed amplification assays is the de novo aggregation propensity of the α-synuclein substrate as well as inter-batch heterogeneity. While much work has focused on determining appropriate seed amplification assay buffer compositions as well as the type and amount of seed used, a robust comparison of α-synuclein substrate purification methods has not been reported. We therefore compared the utility of recombinant α-synuclein purified using four different methods as seed amplification assay substrates across two laboratories. Osmotic shock-purified α-synuclein monomer substrate showed the lowest propensity for de novo aggregation, which translated into being the best substrate for seed amplification assay reactions seeded with α-synuclein preformed fibrils or patient brain homogenates. Furthermore, osmotic shock α-synuclein monomer showed the best inter-batch reproducibility compared to all other substrates tested. As α-synuclein seed amplification assays continue to evolve and move towards adoption in the clinical realm, this work showcases the vital importance of standardizing the production and characterization of recombinant α-synuclein substrate. We encourage the widespread adoption of osmotic shock α-synuclein monomer as the universal substrate for seed amplification assays to maximize intra- and inter-laboratory reproducibility.
Authors
- Martin Ingelsson (ORCID: https://orcid.org/0000-0001-5466-8370)
- Joel C. Watts (ORCID: https://orcid.org/0000-0002-2604-2925)
- Thomas M. Durcan (ORCID: https://orcid.org/0000-0003-3942-1956)
- Jean‐François Trempe (ORCID: https://orcid.org/0000-0002-6543-3371)
- Edward A. Fon (ORCID: https://orcid.org/0000-0002-5520-6239)
- Irina Shlaifer (ORCID: https://orcid.org/0000-0002-3737-268X)
- Zaid A.M. Al‐Azzawi (ORCID: https://orcid.org/0000-0002-6200-8986)
- Nicholas R. G. Silver (ORCID: https://orcid.org/0000-0002-2199-3123)
- Bradley T. Hyman (ORCID: https://orcid.org/0000-0002-7959-9401)
- Surabhi Mehra (ORCID: https://orcid.org/0000-0003-1777-673X)
- Shuqiong Niu (ORCID: https://orcid.org/0000-0001-7004-3768)
- Wen Luo (ORCID: https://orcid.org/0000-0002-7551-5629)
- Christopher Situ
Institutions
- Uppsala University (SE)
- Montreal Neurological Institute and Hospital (CA)
- University Health Network (CA)
- Harvard University (US)
- University of Toronto (CA)
- Massachusetts General Hospital (US)
- Occupational Cancer Research Centre (CA)
- Ontario Brain Institute (CA)
- McGill University (CA)
Publication Details
- Journal
- Acta Neuropathologica Communications
- Published
- 2025-11-05
- DOI
- https://doi.org/10.1186/s40478-025-02151-4
- Citations
- 1
- Primary Topic
- Parkinson's Disease Mechanisms and Treatments
- Type
- article
- Field-Weighted Citation Impact
- 1.39
Funders
- McGill University
- Government of Canada
- Parkinson Canada
- Canadian Institutes of Health Research