ArticlePLoS pathogens2017
Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Genetic variability of the prion protein gene (PRNP) in thin-tailed and fat-tailed sheep.Open veterinary journal · 2025Article
- The dynamics of prion spreading is governed by the interplay between the non-linearities of tissue response and replication kinetics.iScience · 2024Article
- Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier.Cell and tissue research · 2023Review
- Homodimeric complexes of the 90-231 human prion: a multilayered computational study based on FMO/GRID-DRY approach.Journal of molecular modeling · 2022Article
- Pentosan polysulfate induces low-level persistent prion infection keeping measurable seeding activity without PrP-res detection in Fukuoka-1 infected cell cultures.Scientific reports · 2022Article
- Asymmetric-flow field-flow fractionation of prions reveals a strain-specific continuum of quaternary structures with protease resistance developing at a hydrodynamic radius of 15 nm.PLoS pathogens · 2021Article
- Prion potentiation after life-long dormancy in mice devoid of PrP.Brain communications · 2021Article
- A seven-residue deletion in PrP leads to generation of a spontaneous prion formed from C-terminal C1 fragment of PrP.The Journal of biological chemistry · 2020Article
- Host prion protein expression levels impact prion tropism for the spleen.PLoS pathogens · 2020Article
- Crossing Species Barriers Relies on Structurally Distinct Prion Assemblies and Their Complementation.Molecular neurobiology · 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
- Transient multimers modulate conformer abundances of prion protein monomer through conformational selection.Scientific reports · 2019Article
- Review
- Review
- High-Pressure Response of Amyloid Folds.Viruses · 2019Review
- Generalizing a mathematical model of prion aggregation allows strain coexistence and co-stability by including a novel misfolded species.Journal of mathematical biology · 2019Article
- Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway.Communications biology · 2019Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian prions, the pathogens that cause transmissible spongiform encephalopathies, propagate by self-perpetuating the structural information stored in the abnormally folded, aggregated conformer (PrPSc) of the host-encoded prion protein (PrPC). To date, no structural model related to prion assembly organization satisfactorily describes how strain-specified structural information is encoded and by which mechanism this information is transferred to PrPC. To achieve progress on this issue, we correlated the PrPSc quaternary structural transition from three distinct prion strains during unfolding and refolding with their templating activity. We reveal the existence of a mesoscopic organization in PrPSc through the packing of a highly stable oligomeric elementary subunit (suPrP), in which the strain structural determinant (SSD) is encoded. Once kinetically trapped, this elementary subunit reversibly loses all replicative information. We demonstrate that acquisition of the templating interface and infectivity requires structural rearrangement of suPrP, in concert with its condensation. The existence of such an elementary brick scales down the SSD support to a small oligomer and provide a basis of reflexion for prion templating process and propagation.
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