Category: Parkinson's Disease: Disease mechanisms
Objective: To investigate the modulatory effects of bacterial-derived proteins on the pathological aggregation of α-synuclein (α-syn)
Background: Aggregation of α-syn into toxic oligomers and protofibrils is a central pathogenic mechanism in Parkinson’s disease (PD). While proteolytic cleavage by human proteases generates fragments with distinct roles, the impact of microbial proteases on this prionoid protein remains unexplored.
Method: Escherichia coli-derived curli assembly protein (CsgC) and Cutibacterium acnes-derived serine protease 3 (CSPS3) were synthesized de novo. Aggregation kinetics of 10 μM human recombinant α-syn (± CSPS3/CsgC) were evaluated using a thioflavin-T (ThT) fluorescence assay over 360 minutes at 37°C. Conformational changes were assessed via a Congo red (CR) spectroscopic assay (absorbance 400–650 nm). Morphological characterization utilized transmission electron microscopy (TEM) with uranyl acetate negative staining at 120 kV.
Results: CSPS3 caused a dose-dependent reduction in the ThT fluorescence signal of α-syn. This was supported by the CR assay, showing a distinct shift in the absorption maximum from 510 nm in the presence of CSPS3. TEM imaging revealed that CSPS3-treated α-syn samples formed fewer and smaller aggregates versus untreated controls. Furthermore, CsgC inhibited α-syn aggregation but not amyloid-beta 42 (Aβ42) fibrillation, indicating client-specific selectivity.
Conclusion: The bacterial serine protease CSPS3 and curli assembly protein CsgC effectively inhibit in vitro α-syn fibrillation. This provides the first evidence that microbial proteins can modify the α-syn pathological aggregation process. These findings support investigating bacterial-derived proteins as potential PD therapeutic candidates.
References: 1. Iwata A, Maruyama M, Akagi T, et al. Hum Mol Genet 2003;12:2625–35.
2. Sung JY, Park SM, Lee CH, et al. J Biol Chem 2005;280:25216–24.
3. Evans ML, Chorell E, Taylor JD, et al. Mol Cell 2015;57:445-55.
4. Palacios N, Wilkinson J, Bjornevik K, et al. Ann Neurol 2023;94:486–501.
5. Klein RD, Shu Q, Cusumano ZT, et al. mBio 2018;9:e01349–18.
To cite this abstract in AMA style:
HJ. Yang, JI. Choi. Modulatory effects of bacterial-derived serine protease on pathological α-synuclein fibrillation in vitro [abstract]. Mov Disord. 2026; 41 (suppl 1). https://www.mdsabstracts.org/abstract/modulatory-effects-of-bacterial-derived-serine-protease-on-pathological-%ce%b1-synuclein-fibrillation-in-vitro/. Accessed October 1, 2026.« Back to 2026 International Congress
MDS Abstracts - https://www.mdsabstracts.org/abstract/modulatory-effects-of-bacterial-derived-serine-protease-on-pathological-%ce%b1-synuclein-fibrillation-in-vitro/
