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

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Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation. / Andersen, Kell K; Vad, Brian S; Kjaer, Lars; Tolker-Nielsen, Tim; Christiansen, Gunna; Otzen, Daniel E.

I: FEBS Letters, Bind 592, Nr. 9, 05.2018, s. 1484-1496.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Andersen, Kell K ; Vad, Brian S ; Kjaer, Lars ; Tolker-Nielsen, Tim ; Christiansen, Gunna ; Otzen, Daniel E. / Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation. I: FEBS Letters. 2018 ; Bind 592, Nr. 9. s. 1484-1496.

Bibtex

@article{40d02970b47b4b98b4c822811d2e0290,
title = "Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation",
abstract = "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.",
author = "Andersen, {Kell K} and Vad, {Brian S} and Lars Kjaer and Tim Tolker-Nielsen and Gunna Christiansen and Otzen, {Daniel E}",
note = "This article is protected by copyright. All rights reserved.",
year = "2018",
month = "5",
doi = "10.1002/1873-3468.13038",
language = "English",
volume = "592",
pages = "1484--1496",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "9",

}

RIS

TY - JOUR

T1 - Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation

AU - Andersen, Kell K

AU - Vad, Brian S

AU - Kjaer, Lars

AU - Tolker-Nielsen, Tim

AU - Christiansen, Gunna

AU - Otzen, Daniel E

N1 - This article is protected by copyright. All rights reserved.

PY - 2018/5

Y1 - 2018/5

N2 - 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.

AB - 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.

U2 - 10.1002/1873-3468.13038

DO - 10.1002/1873-3468.13038

M3 - Journal article

VL - 592

SP - 1484

EP - 1496

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 9

ER -