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TitleStochastic misfolding drives the emergence of distinct α-synuclein strains.
Journal, issue, pagesNeuron, Year 2026
Publish dateFeb 27, 2026
AuthorsRaphaella W L So / Benedikt Frieg / José D Camino / Christopher Situ / Mark N Metri / Nicholas R G Silver / Le Yao Li / Alison Mao / Erica Stuart / Gunnar F Schröder / Joel C Watts /
PubMed Abstractα-Synuclein conformational strains provide a potential explanation for the clinical and pathological differences among synucleinopathies such as Parkinson's disease and multiple system atrophy. ...α-Synuclein conformational strains provide a potential explanation for the clinical and pathological differences among synucleinopathies such as Parkinson's disease and multiple system atrophy. However, how distinct α-synuclein strains arise remains unknown. Here, we observed conformational heterogeneity between individual preparations of α-synuclein pre-formed fibrils (PFFs) generated by polymerizing wild-type or A53T-mutant human α-synuclein under identical conditions. Moreover, we found that α-synuclein aggregates formed spontaneously in the brains of a transgenic synucleinopathy mouse model are conformationally diverse. Propagation of stochastically formed PFF- and brain-derived α-synuclein strains in mice initiated several distinct synucleinopathies. The conformational diversity of α-synuclein aggregates across PFF preparations and between individual mice demonstrates that α-synuclein can spontaneously form multiple self-propagating strains within an identical environment. This suggests that stochastic misfolding into distinct aggregate structures drives the emergence of α-synuclein strains and reveals that the intrinsic variability of common synucleinopathy research tools must be considered when designing and interpreting experiments.
External linksNeuron / PubMed:41763203
MethodsEM (helical sym.)
Resolution3.02 - 3.64 Å
Structure data

53884

9rb3

EMDB-53884, PDB-9rb3:
A53T alpha-synuclein fibril - Type 1
Method: EM (helical sym.) / Resolution: 3.4 Å

53885

9rb6

EMDB-53885, PDB-9rb6:
A53T alpha-synuclein fibril - Type 2
Method: EM (helical sym.) / Resolution: 3.02 Å

53886

9rb7

EMDB-53886, PDB-9rb7:
Wild-type alpha-synuclein fibril - Type 1
Method: EM (helical sym.) / Resolution: 3.45 Å

53887

9rb8

EMDB-53887, PDB-9rb8:
Wild-type alpha-synuclein fibril - Type 3-1
Method: EM (helical sym.) / Resolution: 3.64 Å

53888

9rb9

EMDB-53888, PDB-9rb9:
Wild-type alpha-synuclein fibril - Type 3-2
Method: EM (helical sym.) / Resolution: 3.04 Å

53889

9rba

EMDB-53889, PDB-9rba:
Wild-type alpha-synuclein fibril - Type 4
Method: EM (helical sym.) / Resolution: 3.54 Å

53890

9rbb

EMDB-53890, PDB-9rbb:
Wild-type alpha-synuclein fibril - Type 5
Method: EM (helical sym.) / Resolution: 3.15 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / alpha-synuclein / fibril / A53T mutant

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