ArticleJournal of molecular biology2011
Conformational transformation and selection of synthetic prion strains.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 papers.
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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.
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Who cites it
40 citing papers in PubMed, 53 citations in OpenAlex.
- Trial
- Article
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- Brain-derived tau oligomer polymorphs: distinct aggregations, stability profiles, and biological activities.Communications biology · 2025Article
- α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model.PLoS pathogens · 2024Article
- Effect of Natural Osmolytes on Recombinant Tau Monomer: Propensity of Oligomerization and Aggregation.ACS chemical neuroscience · 2024Article
- Efficient interspecies transmission of synthetic prions.PLoS pathogens · 2021Article
- Modulating disease-relevant tau oligomeric strains by small molecules.The Journal of biological chemistry · 2020Article
- Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration.Viruses · 2019Review
- Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019Review
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Molecular Mechanisms of Chronic Wasting Disease Prion Propagation.Cold Spring Harbor perspectives in medicine · 2018Review
- Evolutionary biology and the risk of scrapie disease in sheep.Open veterinary journal · 2018Review
- Strains of Pathological Protein Aggregates in Neurodegenerative Diseases.Discoveries (Craiova, Romania) · 2017Review
- Biology and Genetics of PrP Prion Strains.Cold Spring Harbor perspectives in medicine · 2017Review
- Prion Strain Diversity.Cold Spring Harbor perspectives in medicine · 2016Review
- Proteopathic Strains and the Heterogeneity of Neurodegenerative Diseases.Annual review of genetics · 2016Review
- Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner.The Journal of biological chemistry · 2016Article
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.The American journal of pathology · 2016Article
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Prion protein is capable of folding into multiple self-replicating prion strains that produce phenotypically distinct neurological disorders. Although prion strains often breed true upon passage, they can also transform or "mutate" despite being devoid of nucleic acids. To dissect the mechanism of prion strain transformation, we studied the physicochemical evolution of a mouse synthetic prion (MoSP) strain, MoSP1, after repeated passage in mice and cultured cells. We show that MoSP1 gradually adopted shorter incubation times and lower conformational stabilities. These changes were accompanied by structural transformation, as indicated by a shift in the molecular mass of the protease-resistant core of MoSP1 from approximately 19 kDa [MoSP1(2)] to 21 kDa [MoSP1(1)]. We show that MoSP1(1) and MoSP1(2) can breed with fidelity when cloned in cells; however, when present as a mixture, MoSP1(1) preferentially proliferated, leading to the disappearance of MoSP1(2). In culture, the rate of this transformation process can be influenced by the composition of the culture media and the presence of polyamidoamines. Our findings demonstrate that prions can exist as a conformationally diverse population of strains, each capable of replicating with high fidelity. Rare conformational conversion, followed by competitive selection among the resulting pool of conformers, provides a mechanism for the adaptation of the prion population to its host environment.
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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.