ArticlePLoS pathogens2019
Development of a new largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- D178N prion protein mutation endows RML prions with new strain properties that do not mimic human genetic prion diseases.Acta neuropathologica · 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
- Multiple Antibody-Coated Gold Nanoparticle-Based ExoAssay for Rapid Isolation of CNS-Specific Exosomes From Blood.Journal of neurochemistry · 2025Article
- Effect of primary structural variation on cervid prion protein in flexibility, stability, and spontaneous misfolding propensity.Neurobiology of disease · 2025Article
- Conservation of strain properties of bank vole-adapted chronic wasting disease in the absence of glycosylation and membrane anchoring.Neurobiology of disease · 2025Article
- The Evolution of Experimental Rodent Models for Prion Diseases.Journal of neurochemistry · 2025Review
- The molecular determinants of a universal prion acceptor.PLoS pathogens · 2024Article
- Convergent generation of atypical prions in knockin mouse models of genetic prion disease.The Journal of clinical investigation · 2024Article
- A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions.Nature communications · 2024Article
- RNA-Seq Analysis of Mammalian Prion Disease.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A tetracationic porphyrin with dual anti-prion activity.iScience · 2023Article
- Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generation.Acta neuropathologica communications · 2023Article
- Development of a methodology for large-scale production of prions for biological and structural studies.Frontiers in molecular biosciences · 2023Article
- Conformational diversity in purified prions produced in vitro.PLoS pathogens · 2023Article
- Bona fide atypical scrapie faithfully reproduced for the first time in a rodent model.Acta neuropathologica communications · 2022Article
- Review
- Pharmacological inactivation of the prion protein by targeting a folding intermediate.Communications biology · 2021Article
- Detection of Pathognomonic Biomarker PrPBiomolecules · 2020Review
- 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
- A Novel, Reliable and Highly Versatile Method to Evaluate Different Prion Decontamination Procedures.Frontiers in bioengineering and biotechnology · 2020Article
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Authors and funding
25 authors.
Funding
Abstract
The resolution of the three-dimensional structure of infectious prions at the atomic level is pivotal to understand the pathobiology of Transmissible Spongiform Encephalopathies (TSE), but has been long hindered due to certain particularities of these proteinaceous pathogens. Difficulties related to their purification from brain homogenates of disease-affected animals were resolved almost a decade ago by the development of in vitro recombinant prion propagation systems giving rise to highly infectious recombinant prions. However, lack of knowledge about the molecular mechanisms of the misfolding event and the complexity of systems such as the Protein Misfolding Cyclic Amplification (PMCA), have limited generating the large amounts of homogeneous recombinant prion preparations required for high-resolution techniques such as solid state Nuclear Magnetic Resonance (ssNMR) imaging. Herein, we present a novel recombinant prion propagation system based on PMCA that substitutes sonication with shaking thereby allowing the production of unprecedented amounts of multi-labeled, infectious recombinant prions. The use of specific cofactors, such as dextran sulfate, limit the structural heterogeneity of the in vitro propagated prions and makes possible, for the first time, the generation of infectious and likely homogeneous samples in sufficient quantities for studies with high-resolution structural techniques as demonstrated by the preliminary ssNMR spectrum presented here. Overall, we consider that this new method named Protein Misfolding Shaking Amplification (PMSA), opens new avenues to finally elucidate the three-dimensional structure of infectious prions.
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