ArticlePLoS pathogens2011
Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed, 104 citations in OpenAlex.
- Limited transmission of cervid prions to nonhuman primates provides insights into the zoonotic potential of chronic wasting disease.Science advances · 2026Article
- Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties.Acta neuropathologica communications · 2025Article
- Cofactors facilitate bona fide prion misfolding in vitro but are not necessary for the infectivity of recombinant murine prions.PLoS pathogens · 2025Article
- A-synuclein prion strains differentially adapt after passage in mice.PLoS pathogens · 2024Article
- Structurally targeted mutagenesis identifies key residues supporting α-synuclein misfolding in multiple system atrophy.Journal of Parkinson's disease · 2024Article
- Propagation of distinct CWD prion strains during peripheral and intracerebral challenges of gene-targeted mice.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structurally targeted mutagenesis identifies key residues supportingbioRxiv : the preprint server for biology · 2024Article
- Multiple steps of prion strain adaptation to a new host.Frontiers in neuroscience · 2024Article
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier.Cell and tissue research · 2023Review
- Review
- Fibrinogen Mitigates Prion-Mediated Platelet Activation and Neuronal Cell Toxicity.Frontiers in cell and developmental biology · 2022Article
- Review
- Efficient interspecies transmission of synthetic prions.PLoS pathogens · 2021Article
- The degree of astrocyte activation is predictive of the incubation time to prion disease.Acta neuropathologica communications · 2021Article
- From Posttranslational Modifications to Disease Phenotype: A Substrate Selection Hypothesis in Neurodegenerative Diseases.International journal of molecular sciences · 2021Review
- Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays.Biomolecules · 2020Review
- Oral Ingestion of Synthetically Generated Recombinant Prion Is Sufficient to Cause Prion Disease in Wild-Type Mice.Pathogens (Basel, Switzerland) · 2020Article
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Isolation of infectious, non-fibrillar and oligomeric prions from a genetic prion disease.Brain : a journal of neurology · 2020Article
22 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transmissible agent of prion disease consists of a prion protein in its abnormal, β-sheet rich state (PrP(Sc)), which is capable of replicating itself according to the template-assisted mechanism. This mechanism postulates that the folding pattern of a newly recruited polypeptide chain accurately reproduces that of a PrP(Sc) template. Here we report that authentic PrP(Sc) and transmissible prion disease can be generated de novo in wild type animals by recombinant PrP (rPrP) amyloid fibrils, which are structurally different from PrP(Sc) and lack any detectable PrP(Sc) particles. When induced by rPrP fibrils, a long silent stage that involved two serial passages preceded development of the clinical disease. Once emerged, the prion disease was characterized by unique clinical, neuropathological, and biochemical features. The long silent stage to the disease was accompanied by significant transformation in neuropathological properties and biochemical features of the proteinase K-resistant PrP material (PrPres) before authentic PrP(Sc) evolved. The current work illustrates that transmissible prion diseases can be induced by PrP structures different from that of authentic PrP(Sc) and suggests that a new mechanism different from the classical templating exists. This new mechanism designated as "deformed templating" postulates that a change in the PrP folding pattern from the one present in rPrP fibrils to an alternative specific for PrP(Sc) can occur. The current work provides important new insight into the mechanisms underlying genesis of the transmissible protein states and has numerous implications for understanding the etiology of neurodegenerative diseases.
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