ArticlePloS one2013
Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 46 citations in OpenAlex.
- 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
- Article
- A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions.Nature communications · 2024Article
- 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
- Essential Components of Synthetic Infectious Prion Formation De Novo.Biomolecules · 2022Review
- Review
- Reduced Expression of Prion Protein With Increased Interferon-β Fail to Limit Creutzfeldt-Jakob Disease Agent Replication in Differentiating Neuronal Cells.Frontiers in physiology · 2022Article
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Development of a new largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies.PLoS pathogens · 2019Article
- Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019Review
- RNA modulates aggregation of the recombinant mammalian prion protein by direct interaction.Scientific reports · 2019Article
- Structural attributes of mammalian prion infectivity: Insights from studies with synthetic prions.The Journal of biological chemistry · 2018Article
- A quantitative characterization of interaction between prion protein with nucleic acids.Biochemistry and biophysics reports · 2018Article
- Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Molecular psychiatry · 2018Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- Experimental transfusion of variant CJD-infected blood reveals previously uncharacterised prion disorder in mice and macaque.Nature communications · 2017Article
- Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome.Scientific reports · 2017Article
- Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity.PLoS pathogens · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
During prion infection, the normal, protease-sensitive conformation of prion protein (PrP(C)) is converted via seeded polymerization to an abnormal, infectious conformation with greatly increased protease-resistance (PrP(Sc)). In vitro, protein misfolding cyclic amplification (PMCA) uses PrP(Sc) in prion-infected brain homogenates as an initiating seed to convert PrP(C) and trigger the self-propagation of PrP(Sc) over many cycles of amplification. While PMCA reactions produce high levels of protease-resistant PrP, the infectious titer is often lower than that of brain-derived PrP(Sc). More recently, PMCA techniques using bacterially derived recombinant PrP (rPrP) in the presence of lipid and RNA but in the absence of any starting PrP(Sc) seed have been used to generate infectious prions that cause disease in wild-type mice with relatively short incubation times. These data suggest that lipid and/or RNA act as cofactors to facilitate the de novo formation of high levels of prion infectivity. Using rPrP purified by two different techniques, we generated a self-propagating protease-resistant rPrP molecule that, regardless of the amount of RNA and lipid used, had a molecular mass, protease resistance and insolubility similar to that of PrP(Sc). However, we were unable to detect prion infectivity in any of our reactions using either cell-culture or animal bioassays. These results demonstrate that the ability to self-propagate into a protease-resistant insoluble conformer is not unique to infectious PrP molecules. They suggest that the presence of RNA and lipid cofactors may facilitate the spontaneous refolding of PrP into an infectious form while also allowing the de novo formation of self-propagating, but non-infectious, rPrP-res.
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