ArticleThe Journal of biological chemistry2022
Mechanistic insights into accelerated α-synuclein aggregation mediated by human microbiome-associated functional amyloids.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Aggregation in gut: on the link between neurodegeneration and bacterial functional amyloids.NPJ biofilms and microbiomes · 2026Article
- Gut microbiota and Parkinson's disease: exploring pathogenesis and potential therapeutic strategies from a gut-brain axis perspective.iScience · 2026Review
- Silent Intruders: The Gut Virome in Brain Aging and Cognitive Decline.Pathogens (Basel, Switzerland) · 2026Review
- Transient binding facilitates super-resolution imaging of functional amyloid fibrils on living bacteria.Protein science : a publication of the Protein Society · 2026Article
- Microbiota-Gut-Brain Axis in Neurodegenerative Diseases: The Role of Bacterial Amyloids.Cellular and molecular gastroenterology and hepatology · 2026Review
- Artificial intelligence empowers gut microbiota research in neurodegenerative diseases molecular mechanisms and precision therapy.iScience · 2025Review
- The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Exogenous prion-like proteins and their potential to trigger cognitive dysfunction.Molecular systems biology · 2025Article
- Article
- Parkinson's Disease and the Microbiota-Gut-Brain Axis: Metabolites, Mechanisms, and Innovative Therapeutic Strategies Targeting the Gut Microbiota.Molecular neurobiology · 2025Review
- Lewy body diseases and the gut.Molecular neurodegeneration · 2025Review
- Helicobacter pylori outer membrane vesicles directly promote Aβ aggregation and enhance Aβ toxicity in APP/PS1 mice.Communications biology · 2024Article
- Gut-first Parkinson's disease is encoded by gut dysbiome.Molecular neurodegeneration · 2024Article
- The menace within: bacterial amyloids as a trigger for autoimmune and neurodegenerative diseases.Current opinion in microbiology · 2024Review
- Pathways linking microbiota-gut-brain axis with neuroinflammatory mechanisms in Alzheimer's pathophysiology.Microbiome research reports · 2024Review
- PACT - Prediction of amyloid cross-interaction by threading.Scientific reports · 2023Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Digestive exophagy of biofilms by intestinal amoeba and its impact on stress tolerance and cytotoxicity.NPJ biofilms and microbiomes · 2023Article
- Structural analysis and architectural principles of the bacterial amyloid curli.Nature communications · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The gut microbiome has been shown to have key implications in the pathogenesis of Parkinson's disease (PD). The Escherichia coli functional amyloid CsgA is known to accelerate α-synuclein aggregation in vitro and induce PD symptoms in mice. However, the mechanism governing CsgA-mediated acceleration of α-synuclein aggregation is unclear. Here, we show that CsgA can form stable homodimeric species that correlate with faster α-synuclein amyloid aggregation. Furthermore, we identify and characterize new CsgA homologs encoded by bacteria present in the human microbiome. These CsgA homologs display diverse aggregation kinetics, and they differ in their ability to modulate α-synuclein aggregation. Remarkably, we demonstrate that slowing down CsgA aggregation leads to an increased acceleration of α-synuclein aggregation, suggesting that the intrinsic amyloidogenicity of gut bacterial CsgA homologs affects their ability to accelerate α-synuclein aggregation. Finally, we identify a complex between CsgA and α-synuclein that functions as a platform to accelerate α-synuclein aggregation. Taken together, our work reveals complex interplay between bacterial amyloids and α-synuclein that better informs our understanding of PD causation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.