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Structural and functional characterization of two alpha-synuclein strains

Author

Listed:
  • 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)

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.

Suggested Citation

  • Luc Bousset & Laura Pieri & Gemma Ruiz-Arlandis & Julia Gath & Poul Henning Jensen & Birgit Habenstein & Karine Madiona & Vincent Olieric & Anja Böckmann & Beat H. Meier & Ronald Melki, 2013. "Structural and functional characterization of two alpha-synuclein strains," Nature Communications, Nature, vol. 4(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3575
    DOI: 10.1038/ncomms3575
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    Cited by:

    1. Derya Emin & Yu P. Zhang & Evgeniia Lobanova & Alyssa Miller & Xuecong Li & Zengjie Xia & Helen Dakin & Dimitrios I. Sideris & Jeff Y. L. Lam & Rohan T. Ranasinghe & Antonina Kouli & Yanyan Zhao & Sum, 2022. "Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Jemil Ahmed & Tessa C. Fitch & Courtney M. Donnelly & Johnson A. Joseph & Tyler D. Ball & Mikaela M. Bassil & Ahyun Son & Chen Zhang & Aurélie Ledreux & Scott Horowitz & Yan Qin & Daniel Paredes & Sun, 2022. "Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    3. Dhruva D. Dhavale & Alexander M. Barclay & Collin G. Borcik & Katherine Basore & Deborah A. Berthold & Isabelle R. Gordon & Jialu Liu & Moses H. Milchberg & Jennifer Y. O’Shea & Michael J. Rau & Zacha, 2024. "Structure of alpha-synuclein fibrils derived from human Lewy body dementia tissue," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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