ArticleProtein science : a publication of the Protein Society2021
Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Biofilm-associated proteins: from the gut biofilms to neurodegeneration.Gut microbes · 2025Review
- Natural Design of a Stabilized Cross-β Fold: Structure of the FuA FapC from Pseudomonas Sp. UK4 Reveals a Critical Role for Stacking of Imperfect Repeats.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Neurodegenerative diseases: from gut-brain axis to brain microbiome.Frontiers in aging neuroscience · 2023Article
- Trans-seeding of Alzheimer-related tau protein by a yeast prion.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Article
- Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats.Protein science : a publication of the Protein Society · 2021Article
- Co-Aggregation of S100A9 with DOPA and Cyclen-Based Compounds Manifested in Amyloid Fibril Thickening without Altering Rates of Self-Assembly.International journal of molecular sciences · 2021Article
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Authors and funding
7 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
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 (PD). 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 PD transgenic rats and their wild type counterparts, based on their stability against dissolution by formic acid (FA). 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 FA, 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 FA to identify amyloidogenic protein in complex mixtures and suggests that there may be numerous functional amyloid proteins in microbiomes.
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