ArticleOpen biology2015
A systematic investigation of production of synthetic prions from recombinant prion protein.
Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- Strain-specific propagation of variant Creutzfeldt-Jakob disease prions in humanized neural cells.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Intracellular trafficking SNARE protein, syntaxin-6, modifies prion cellular phenotypes and risk of disease development in vivo.Acta neuropathologica · 2025Article
- Article
- Screening of Anti-Prion Compounds Using the Protein Misfolding Cyclic Amplification Technology.Biomolecules · 2024Article
- Article
- Prion protein conversion at two distinct cellular sites precedes fibrillisation.Nature communications · 2023Article
- A structural basis for prion strain diversity.Nature chemical biology · 2023Article
- Prion strains viewed through the lens of cryo-EM.Cell and tissue research · 2023Review
- Development of a methodology for large-scale production of prions for biological and structural studies.Frontiers in molecular biosciences · 2023Article
- Essential Components of Synthetic Infectious Prion Formation De Novo.Biomolecules · 2022Review
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- 2.7 Å cryo-EM structure of ex vivo RML prion fibrils.Nature communications · 2022Article
- Highly infectious prions are not directly neurotoxic.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Proteopathic Seed Amplification Assays for Neurodegenerative Disorders.Clinics in laboratory medicine · 2020Review
- Crossing Species Barriers Relies on Structurally Distinct Prion Assemblies and Their Complementation.Molecular neurobiology · 2020Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro.Scientific reports · 2019Article
- Recent Advances in Understanding Mammalian Prion Structure: A Mini Review.Frontiers in molecular neuroscience · 2019Article
- A simple in vitro assay for assessing the efficacy, mechanisms and kinetics of anti-prion fibril compounds.Prion · 2018Article
Corrections and comments
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Authors and funding
20 authors at 4 institutions in 2 countries.
Funding
Abstract
According to the protein-only hypothesis, infectious mammalian prions, which exist as distinct strains with discrete biological properties, consist of multichain assemblies of misfolded cellular prion protein (PrP). A critical test would be to produce prion strains synthetically from defined components. Crucially, high-titre 'synthetic' prions could then be used to determine the structural basis of infectivity and strain diversity at the atomic level. While there have been multiple reports of production of prions from bacterially expressed recombinant PrP using various methods, systematic production of high-titre material in a form suitable for structural analysis remains a key goal. Here, we report a novel high-throughput strategy for exploring a matrix of conditions, additives and potential cofactors that might generate high-titre prions from recombinant mouse PrP, with screening for infectivity using a sensitive automated cell-based bioassay. Overall, approximately 20,000 unique conditions were examined. While some resulted in apparently infected cell cultures, this was transient and not reproducible. We also adapted published methods that reported production of synthetic prions from recombinant hamster PrP, but again did not find evidence of significant infectious titre when using recombinant mouse PrP as substrate. Collectively, our findings are consistent with the formation of prion infectivity from recombinant mouse PrP being a rare stochastic event and we conclude that systematic generation of prions from recombinant PrP may only become possible once the detailed structure of authentic ex vivo prions is solved.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.