ArticleScientific reports2016
Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Amplification of seeding-competent tau aggregates by PMCA in human and experimental tauopathies.Acta neuropathologica communications · 2026Article
- Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier.Cell and tissue research · 2023Review
- Essential Components of Synthetic Infectious Prion Formation De Novo.Biomolecules · 2022Review
- Glycans are not necessary to maintain the pathobiological features of bovine spongiform encephalopathy.PLoS pathogens · 2022Article
- Site-specific analysis of N-glycans from different sheep prion strains.PLoS pathogens · 2021Article
- Methionine oxidation within the prion protein.Prion · 2020Review
- Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.The Journal of biological chemistry · 2020Article
- Improving the Predictive Value of Prion Inactivation Validation Methods to Minimize the Risks of Iatrogenic Transmission With Medical Instruments.Frontiers in bioengineering and biotechnology · 2020Review
- 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
- Review
- Engineering a murine cell line for the stable propagation of hamster prions.The Journal of biological chemistry · 2019Article
- Recent Advances in Understanding Mammalian Prion Structure: A Mini Review.Frontiers in molecular neuroscience · 2019Article
- Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway.Communications biology · 2019Article
- Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity.Scientific reports · 2018Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Real-time Quaking-induced Conversion Assay for Detection of CWD Prions in Fecal Material.Journal of visualized experiments : JoVE · 2017Article
- Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are formed of misfolded assemblies (PrP(Sc)) of the variably N-glycosylated cellular prion protein (PrP(C)). In infected species, prions replicate by seeding the conversion and polymerization of host PrP(C). Distinct prion strains can be recognized, exhibiting defined PrP(Sc) biochemical properties such as the glycotype and specific biological traits. While strain information is encoded within the conformation of PrP(Sc) assemblies, the storage of the structural information and the molecular requirements for self-perpetuation remain uncertain. Here, we investigated the specific role of PrP(C) glycosylation status. First, we developed an efficient protein misfolding cyclic amplification method using cells expressing the PrP(C) species of interest as substrate. Applying the technique to PrP(C) glycosylation mutants expressing cells revealed that neither PrP(C) nor PrP(Sc) glycoform stoichiometry was instrumental to PrP(Sc) formation and strainness perpetuation. Our study supports the view that strain properties, including PrP(Sc) glycotype are enciphered within PrP(Sc) structural backbone, not in the attached glycans.
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