Andrej Bieri

Current Project

Strain dependent prion-like spreading of ⍺-Synuclein

The accumulation of misfolded alpha-synuclein (α-syn) into insoluble aggregates is a molecular characteristic in several neurodegenerative diseases, in particular, Parkinson’s disease, multiple system atrophy and dementia with Lewy bodies. Recent studies have shown that once α-syn has started to misfold and aggregate the tendency is transmitted from cell-to-cell, thereby recruiting endogenous α-syn and inducing fibrillization in a prion-like manner. Similar to prion diseases, the heterogeneity of protein aggregate conformations may explain the variable efficiency of template fibrillization and propagation of these misfolded proteins. Additionally, the type of structural strain might be disease defining.

In this project, we focus on the cell-to-cell spreading of defined preformed α-syn seeds. Thereby observing the role of the structural features in spreading efficiency, localization in cells and recruitment of endogenous α-syn.

Short Biography

2014-2019, PhD Stud., PostDoc

C-CINA, Biozentrum, Uni Basel, Mattenstrasse 26, Room P36, CH-4058 Basel, Switzerland