ArticleActa neuropathologica communications2015
Two alternative pathways for generating transmissible prion disease de novo.
Article in Acta neuropathologica communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- 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
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different cell tropism.Neurobiology of disease · 2020Article
- Modeling PrPFrontiers in bioengineering and biotechnology · 2020Article
- 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
- Analysis of Covalent Modifications of Amyloidogenic Proteins Using Two-Dimensional Electrophoresis: Prion Protein and Its Sialylation.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Analyses of N-linked glycans of PrPThe FEBS journal · 2017Article
- Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.PLoS pathogens · 2017Article
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
- Sialylation Controls Prion FateThe Journal of biological chemistry · 2017Article
- Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Scientific reports · 2016Article
- Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner.The Journal of biological chemistry · 2016Article
- New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.The American journal of pathology · 2016Article
- Multifaceted Role of Sialylation in Prion Diseases.Frontiers in neuroscience · 2016Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
introductionPrevious studies established that prion disease with unique strain-specific phenotypes could be induced by in vitro-formed recombinant PrP (rPrP) fibrils with structures different from that of authentic prions, or PrP(Sc). To explain the etiology of prion diseases, new mechanism proposed that in animals the transition from rPrP fibrils to PrP(Sc) consists of two main steps: the first involves fibril-induced formation of atypical PrPres, a self-replicating but clinically silent state, and the second consists of atypical PrPres-dependent formation of PrP(Sc) via rare deformed templating events.
resultsIn the current study, atypical PrPres with characteristics similar to those of brain-derived atypical PrPres was generated in vitro. Upon inoculation into animals, in vitro-generated atypical PrPres gave rise to PrP(Sc) and prion disease with a phenotype similar to those induced by rPrP fibrils. Significant differences in the sialylation pattern between atypical PrPres and PrP(Sc) suggested that only a small sub-fraction of the PrP(C) that is acceptable as a substrate for PrP(Sc) could be also recruited by atypical PrPres. This can explain why atypical PrPres replicates slower than PrP(Sc) and why PrP(Sc) outcompetes atypical PrPres.
conclusionsThis study illustrates that transmissible prion diseases with very similar disease phenotypes could be produced via two alternative procedures: direct inoculation of recombinant PrP amyloid fibrils or in vitro-produced atypical PrPres. Moreover, this work showed that preparations of atypical PrPres free of PrP(Sc) can give rise to transmissible diseases in wild type animals and that atypical PrPres generated in vitro is an adequate model for brain-derived atypical PrPres.
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