Structural and functional characterization of two alpha-synuclein strains

Luc Bousset, Laura Pieri, Gemma Ruiz-Arlandis, Julia Gath, Poul Henning Jensen, Birgit Habenstein, Karine Madiona, Vincent Olieric, Anja Böckmann, Beat H. Meier and Ronald Melki ()
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Luc Bousset: Laboratoire d’Enzymologie et Biochimie Structurales, CNRS
Laura Pieri: Laboratoire d’Enzymologie et Biochimie Structurales, CNRS
Gemma Ruiz-Arlandis: Laboratoire d’Enzymologie et Biochimie Structurales, CNRS
Julia Gath: Physical Chemistry, ETH Zurich
Poul Henning Jensen: Aarhus University
Birgit Habenstein: Institut de Biologie et Chimie des Proteines, CNRS/Universite de Lyon 1
Karine Madiona: Laboratoire d’Enzymologie et Biochimie Structurales, CNRS
Vincent Olieric: Swiss Light Source, Paul Scherrer Institute
Anja Böckmann: Institut de Biologie et Chimie des Proteines, CNRS/Universite de Lyon 1
Beat H. Meier: Physical Chemistry, ETH Zurich
Ronald Melki: Laboratoire d’Enzymologie et Biochimie Structurales, CNRS

Nature Communications, 2013, vol. 4, issue 1, 1-13

Abstract: Abstract α-synuclein aggregation is implicated in a variety of diseases including Parkinson’s disease, dementia with Lewy bodies, pure autonomic failure and multiple system atrophy. The association of protein aggregates made of a single protein with a variety of clinical phenotypes has been explained for prion diseases by the existence of different strains that propagate through the infection pathway. Here we structurally and functionally characterize two polymorphs of α-synuclein. We present evidence that the two forms indeed fulfil the molecular criteria to be identified as two strains of α-synuclein. Specifically, we show that the two strains have different structures, levels of toxicity, and in vitro and in vivo seeding and propagation properties. Such strain differences may account for differences in disease progression in different individuals/cell types and/or types of synucleinopathies.

Date: 2013
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DOI: 10.1038/ncomms3575

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