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Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats

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Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. / Christensen, Line Friis Bakmann; Alijanvand, Saeid Hadi; Burdukiewicz, Michał; Herbst, Florian-Alexander; Kjeldal, Henrik; Dueholm, Morten Simonsen; Otzen, Daniel E.

In: Protein Science, 01.06.2021.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Christensen, LFB, Alijanvand, SH, Burdukiewicz, M, Herbst, F-A, Kjeldal, H, Dueholm, MS & Otzen, DE 2021, 'Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats', Protein Science. https://doi.org/10.1002/pro.4137

APA

Christensen, L. F. B., Alijanvand, S. H., Burdukiewicz, M., Herbst, F-A., Kjeldal, H., Dueholm, M. S., & Otzen, D. E. (2021). Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. Protein Science. https://doi.org/10.1002/pro.4137

CBE

Christensen LFB, Alijanvand SH, Burdukiewicz M, Herbst F-A, Kjeldal H, Dueholm MS, Otzen DE. 2021. Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. Protein Science. https://doi.org/10.1002/pro.4137

MLA

Vancouver

Christensen LFB, Alijanvand SH, Burdukiewicz M, Herbst F-A, Kjeldal H, Dueholm MS et al. Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. Protein Science. 2021 Jun 1. https://doi.org/10.1002/pro.4137

Author

Christensen, Line Friis Bakmann ; Alijanvand, Saeid Hadi ; Burdukiewicz, Michał ; Herbst, Florian-Alexander ; Kjeldal, Henrik ; Dueholm, Morten Simonsen ; Otzen, Daniel E. / Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. In: Protein Science. 2021.

Bibtex

@article{4b0a2409b0324329837fca3a83bf87ef,
title = "Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats",
abstract = "Cross-seeding between amyloidogenic proteins in the gut is receiving increasing attention as a possible mechanism for initiation or acceleration of amyloid formation by aggregation-prone proteins such as αSN, which is central in the development of Parkinson's disease. This is particularly pertinent in view of the growing number of functional (i.e. benign and useful) amyloid proteins discovered in bacteria. Here we identify two amyloidogenic proteins, Pr12 and Pr17, in fecal matter from Parkinson's disease transgenic rats and their wild type counterparts, based on their stability against dissolution by formic acid. Both proteins show robust aggregation into ThT-positive aggregates that contain higher-order β-sheets and have a fibrillar morphology, indicative of amyloid proteins. In addition, Pr17 aggregates formed in vitro showed significant resistance against formic acid, suggesting an ability to form highly stable amyloid. Treatment with proteinase K revealed a protected core of approx. 9 kDa. Neither Pr12 nor Pr17, however, affected αSN aggregation in vitro. Thus, amyloidogenicity does not per se lead to an ability to cross-seed fibrillation of αSN. Our results support the use of proteomics and formic acid to identify amyloidogenic protein in complex mixtures and suggests that there may be numerous functional amyloid proteins in microbiomes. This article is protected by copyright. All rights reserved.",
author = "Christensen, {Line Friis Bakmann} and Alijanvand, {Saeid Hadi} and Micha{\l} Burdukiewicz and Florian-Alexander Herbst and Henrik Kjeldal and Dueholm, {Morten Simonsen} and Otzen, {Daniel E}",
note = "{\textcopyright} 2021 The Protein Society.",
year = "2021",
month = jun,
day = "1",
doi = "10.1002/pro.4137",
language = "English",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell Publishing, Inc.",

}

RIS

TY - JOUR

T1 - Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats

AU - Christensen, Line Friis Bakmann

AU - Alijanvand, Saeid Hadi

AU - Burdukiewicz, Michał

AU - Herbst, Florian-Alexander

AU - Kjeldal, Henrik

AU - Dueholm, Morten Simonsen

AU - Otzen, Daniel E

N1 - © 2021 The Protein Society.

PY - 2021/6/1

Y1 - 2021/6/1

N2 - Cross-seeding between amyloidogenic proteins in the gut is receiving increasing attention as a possible mechanism for initiation or acceleration of amyloid formation by aggregation-prone proteins such as αSN, which is central in the development of Parkinson's disease. This is particularly pertinent in view of the growing number of functional (i.e. benign and useful) amyloid proteins discovered in bacteria. Here we identify two amyloidogenic proteins, Pr12 and Pr17, in fecal matter from Parkinson's disease transgenic rats and their wild type counterparts, based on their stability against dissolution by formic acid. Both proteins show robust aggregation into ThT-positive aggregates that contain higher-order β-sheets and have a fibrillar morphology, indicative of amyloid proteins. In addition, Pr17 aggregates formed in vitro showed significant resistance against formic acid, suggesting an ability to form highly stable amyloid. Treatment with proteinase K revealed a protected core of approx. 9 kDa. Neither Pr12 nor Pr17, however, affected αSN aggregation in vitro. Thus, amyloidogenicity does not per se lead to an ability to cross-seed fibrillation of αSN. Our results support the use of proteomics and formic acid to identify amyloidogenic protein in complex mixtures and suggests that there may be numerous functional amyloid proteins in microbiomes. This article is protected by copyright. All rights reserved.

AB - Cross-seeding between amyloidogenic proteins in the gut is receiving increasing attention as a possible mechanism for initiation or acceleration of amyloid formation by aggregation-prone proteins such as αSN, which is central in the development of Parkinson's disease. This is particularly pertinent in view of the growing number of functional (i.e. benign and useful) amyloid proteins discovered in bacteria. Here we identify two amyloidogenic proteins, Pr12 and Pr17, in fecal matter from Parkinson's disease transgenic rats and their wild type counterparts, based on their stability against dissolution by formic acid. Both proteins show robust aggregation into ThT-positive aggregates that contain higher-order β-sheets and have a fibrillar morphology, indicative of amyloid proteins. In addition, Pr17 aggregates formed in vitro showed significant resistance against formic acid, suggesting an ability to form highly stable amyloid. Treatment with proteinase K revealed a protected core of approx. 9 kDa. Neither Pr12 nor Pr17, however, affected αSN aggregation in vitro. Thus, amyloidogenicity does not per se lead to an ability to cross-seed fibrillation of αSN. Our results support the use of proteomics and formic acid to identify amyloidogenic protein in complex mixtures and suggests that there may be numerous functional amyloid proteins in microbiomes. This article is protected by copyright. All rights reserved.

U2 - 10.1002/pro.4137

DO - 10.1002/pro.4137

M3 - Journal article

C2 - 34075639

JO - Protein Science

JF - Protein Science

SN - 0961-8368

ER -