Poul Henning Jensen

Structural and functional characterization of two alpha-synuclein strains

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Luc Bousset, Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
  • ,
  • Laura Pieri
  • ,
  • Gemma Ruiz-Arlandis
  • ,
  • Julia Gath
  • ,
  • Poul Henning Jensen
  • Birgit Habenstein
  • ,
  • Karine Madiona
  • ,
  • Vincent Olieric
  • ,
  • Anja Böckmann
  • ,
  • Beat H Meier
  • ,
  • Ronald Melki
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.
Original languageEnglish
JournalNature Communications
Volume4
Pages (from-to)2575
ISSN2041-1723
DOIs
Publication statusPublished - 2013

See relations at Aarhus University Citationformats

ID: 68522168