Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal article

DOI

The Parkinson's disease-associated protein α-synuclein (αSN) is natively unfolded but its structure can be modulated by membranes and surfactants. The opportunistic pathogen Pseudomonas aeruginosa (PA) produces and secretes the biosurfactant rhamnolipid (RL) which modulates bacterial biofilm. Here, we show that monomeric RL enhances the ability of αSN to permeabilize membranes, while micellar RL rapidly induces protein β-sheet structure with a worm-like fibrillary appearance, which cannot seed RL-free fibrillation but transforms into linear fibrils faster than αSN fibrillating on its own. Exposure to αSN reduces the degree of biofilm formation by PA unless RL is present. Our data suggest that RL interactions with αSN may affect both αSN aggregation and cell toxicity, potentially implicating microbiomic metabolites in the origin and propagation of Parkinson's disease. This article is protected by copyright. All rights reserved.

Original languageEnglish
JournalFEBS letters
Volume592
Issue number9
Pages (from-to)1484-1496
ISSN0014-5793
DOIs
StatePublished - May 2018

See relations at Aarhus University Citationformats

ID: 125557907