α-Synuclein strains cause distinct synucleinopathies after local and systemic administration

W. Peelaerts, L. Bousset, A. Van der Perren, A. Moskalyuk, R. Pulizzi, M. Giugliano, C. Van den Haute, R. Melki () and V. Baekelandt ()
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W. Peelaerts: KU Leuven, Laboratory for Neurobiology and Gene Therapy
L. Bousset: Paris-Saclay Institute of Neuroscience, CNRS
A. Van der Perren: KU Leuven, Laboratory for Neurobiology and Gene Therapy
A. Moskalyuk: Theoretical Neurobiology & Neuroengineering Laboratory, University of Antwerp
R. Pulizzi: Theoretical Neurobiology & Neuroengineering Laboratory, University of Antwerp
M. Giugliano: Theoretical Neurobiology & Neuroengineering Laboratory, University of Antwerp
C. Van den Haute: KU Leuven, Laboratory for Neurobiology and Gene Therapy
R. Melki: Paris-Saclay Institute of Neuroscience, CNRS
V. Baekelandt: KU Leuven, Laboratory for Neurobiology and Gene Therapy

Nature, 2015, vol. 522, issue 7556, 340-344

Abstract: Brain α-synuclein deposits are the hallmark of various distinct neurodegenerative diseases, and it is proposed that α-synuclein assemblies with different structural characteristics or 'strains' (ribbons or fibrils) could account for pathological differences between these diseases; here different human α-synuclein strains are injected into rat brain, and are shown to propagate in a strain-dependent manner and cause different pathological and neurotoxic phenotypes.

Date: 2015
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DOI: 10.1038/nature14547

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