[NSF-02] Intra- & into-the- brain propagation of α-synuclein: significance for the pathogenesis, progression and therapeutic target of Lewy body diseases

[NSF-02-1] Prion-like propagation of alpha-synuclein assemblies in the brain: from Structure to Function

^○Ronald Melki^1,2 (1.Centre National de la Recherche Scientifique (CNRS), France, 2.Paris-Saclay Institute of Neurosciences, France)

Ronald Melki is Director of research at CNRS. He works on protein misfolding and aggregation since 1999. His team was the first to purify in biochemical amounts the yeast prions Ure2p and Sup35p, to assemble them into infectious assemblies, to solve the crystal structure of a prion, to unveil their structural heterogeneity, to characterize their clearance and the cross-talk between molecular chaperones in yeast prion assembly. In 2009, he demonstrated with Ron Kopito (Stanford University) the prion-like propagation of huntingtin Exon 1 assemblies. Since then he demonstrated the prion-like properties of alpha-synuclein assemblies. His team established structural-molecular basis of different synucleinopathies by generating different strains of alpha-synuclein. Ronald Melki chaired from 2009 till 2014 the CNRS Federative Institute, Genome, Transcriptome, Proteome (over 700 scientists). He co-chaired the Laboratory of Enzymology and Structural Biochemistry of CNRS (over 90 scientists) from 2011 till 2014. He is recipient of the Bettencourt Schueller Fondation prize Coups d'Elan pour la Recherche Française and the Grand Prize of the Fondation Simone et Cino Del Duca of the Institut de France for excellence in research on Parkinson’s Disease. His research is aimed to document the molecular processes leading to neurodegenerative disorders and the development of disease-modifying tools.