ArticleScientific reports2019
Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 41 citations in OpenAlex.
- Effect of primary structural variation on cervid prion protein in flexibility, stability, and spontaneous misfolding propensity.Neurobiology of disease · 2025Article
- Screening of Anti-Prion Compounds Using the Protein Misfolding Cyclic Amplification Technology.Biomolecules · 2024Article
- A structural basis for prion strain diversity.Nature chemical biology · 2023Article
- Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.ACS nano · 2023Article
- Prion strains viewed through the lens of cryo-EM.Cell and tissue research · 2023Review
- Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- 2.7 Å cryo-EM structure of ex vivo RML prion fibrils.Nature communications · 2022Article
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM.Science advances · 2021Article
- The ultrastructure of infectious L-type bovine spongiform encephalopathy prions constrains molecular models.PLoS pathogens · 2021Article
- Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases.Biomolecules · 2021Review
- Exposure to hypergravity during zebrafish development alters cartilage material properties and strain distribution.Bone & joint research · 2021Article
- Highly infectious prions are not directly neurotoxic.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays.Biomolecules · 2020Review
- Structural effects of the highly protective V127 polymorphism on human prion protein.Communications biology · 2020Article
- Cryo-EM structure of an amyloid fibril formed by full-length human prion protein.Nature structural & molecular biology · 2020Article
- Spontaneous generation of prions and transmissible PrP amyloid in a humanised transgenic mouse model of A117V GSS.PLoS biology · 2020Article
- Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core.Nature structural & molecular biology · 2020Article
- Immunotherapy against Prion Disease.Pathogens (Basel, Switzerland) · 2020Review
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
Seeded polymerisation of proteins forming amyloid fibres and their spread in tissues has been implicated in the pathogenesis of multiple neurodegenerative diseases: so called "prion-like" mechanisms. While ex vivo mammalian prions, composed of multichain assemblies of misfolded host-encoded prion protein (PrP), act as lethal infectious agents, PrP amyloid fibrils produced in vitro generally do not. The high-resolution structure of authentic infectious prions and the structural basis of prion strain diversity remain unknown. Here we use cryo-electron microscopy and atomic force microscopy to examine the structure of highly infectious PrP rods isolated from mouse brain in comparison to non-infectious recombinant PrP fibrils generated in vitro. Non-infectious recombinant PrP fibrils are 10 nm wide single fibres, with a double helical repeating substructure displaying small variations in adhesive force interactions across their width. In contrast, infectious PrP rods are 20 nm wide and contain two fibres, each with a double helical repeating substructure, separated by a central gap of 8-10 nm in width. This gap contains an irregularly structured material whose adhesive force properties are strikingly different to that of the fibres, suggestive of a distinct composition. The structure of the infectious PrP rods, which cause lethal neurodegeneration, readily differentiates them from all other protein assemblies so far characterised in other neurodegenerative diseases.
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