ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012
A new mechanism for transmissible prion diseases.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 70 citations in OpenAlex.
- Reactive Microglia and Astrocytes as Therapeutic Targets in Prion Diseases.Sub-cellular biochemistry · 2025Review
- Biological Fluid Biomarkers in Human Prion Diseases with a Note on Biosafety.Sub-cellular biochemistry · 2025Review
- The molecular determinants of a universal prion acceptor.PLoS pathogens · 2024Article
- Multiple steps of prion strain adaptation to a new host.Frontiers in neuroscience · 2024Article
- Role of sialylation of N-linked glycans in prion pathogenesis.Cell and tissue research · 2023Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Review
- Review
- Efficient interspecies transmission of synthetic prions.PLoS pathogens · 2021Article
- From Posttranslational Modifications to Disease Phenotype: A Substrate Selection Hypothesis in Neurodegenerative Diseases.International journal of molecular sciences · 2021Review
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Evaluation of an alternative method for production of biodiesel from processed fats derived from Category 1, 2 and 3 animal by-products (submitted by College Proteins).EFSA journal. European Food Safety Authority · 2020Article
- Modeling PrPFrontiers in bioengineering and biotechnology · 2020Article
- Role of prion protein glycosylation in replication of human prions by protein misfolding cyclic amplification.Laboratory investigation; a journal of technical methods and pathology · 2019Article
- Synthetic Prion Selection and Adaptation.Molecular neurobiology · 2019Article
- Prion neurotoxicity.Brain pathology (Zurich, Switzerland) · 2019Review
- Article
- Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology.Viruses · 2018Review
- Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein.Acta neuropathologica communications · 2018Article
- Prion replication environment defines the fate of prion strain adaptation.PLoS pathogens · 2018Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
The transmissible agent of prion disease consists of prion protein (PrP) in β-sheet-rich state (PrP(Sc)) that can replicate its conformation according to a template-assisted mechanism. This mechanism postulates that the folding pattern of a newly recruited polypeptide accurately reproduces that of the PrP(Sc) template. Here, three conformationally distinct amyloid states were prepared in vitro using Syrian hamster recombinant PrP (rPrP) in the absence of cellular cofactors. Surprisingly, no signs of prion infection were found in Syrian hamsters inoculated with rPrP fibrils that resembled PrP(Sc), whereas an alternative amyloid state, with a folding pattern different from that of PrP(Sc), induced a pathogenic process that led to transmissible prion disease. An atypical proteinase K-resistant, transmissible PrP form that resembled the structure of the amyloid seeds was observed during a clinically silent stage before authentic PrP(Sc) emerged. The dynamics between the two forms suggest that atypical proteinase K-resistant PrP (PrPres) gave rise to PrP(Sc). While no PrP(Sc) was found in preparations of fibrils using protein misfolding cyclic amplification with beads (PMCAb), rPrP fibrils gave rise to atypical PrPres in modified PMCAb, suggesting that atypical PrPres was the first product of PrP(C) misfolding triggered by fibrils. The current work demonstrates that a new mechanism responsible for prion diseases different from the PrP(Sc)-templated or spontaneous conversion of PrP(C) into PrP(Sc) exists. This study provides compelling evidence that noninfectious amyloids with a structure different from that of PrP(Sc) could lead to transmissible prion disease. This work has numerous implications for understanding the etiology of prion and other neurodegenerative diseases.
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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.