ArticleThe Journal of biological chemistry2013
Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 53 citations in OpenAlex.
- Ring trial of 2nd generation RT-QuIC diagnostic tests for sporadic CJD.Annals of clinical and translational neurology · 2020Trial
- Rapidly progressive Alzheimer's disease features distinct structures of amyloid-β.Brain : a journal of neurology · 2015Trial
- The Phenotypic Spectrum of Sporadic Creutzfeldt-Jakob Disease Cortical Subtype.Annals of neurology · 2026Article
- Efficient transmission of human prion diseases to a glycan-free prion protein-expressing host.Brain : a journal of neurology · 2024Article
- Evolving prion-like tau conformers differentially alter postsynaptic proteins in neurons inoculated with distinct isolates of Alzheimer's disease tau.Cell & bioscience · 2023Article
- Evidence for preexisting prion substrain diversity in a biologically cloned prion strain.PLoS pathogens · 2023Article
- A novel subtype of sporadic Creutzfeldt-Jakob disease with PRNP codon 129MM genotype and PrP plaques.Acta neuropathologica · 2023Article
- Emergence of CWD strains.Cell and tissue research · 2023Review
- Glycans are not necessary to maintain the pathobiological features of bovine spongiform encephalopathy.PLoS pathogens · 2022Article
- Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer's disease.Science translational medicine · 2022Article
- Detection of two dissimilar chronic wasting disease isolates in two captive Rocky Mountain elk (Prion · 2021Article
- Distinct conformers of amyloid beta accumulate in the neocortex of patients with rapidly progressive Alzheimer's disease.The Journal of biological chemistry · 2021Article
- Structural and Functional Insights into α-Synuclein Fibril Polymorphism.Biomolecules · 2021Review
- Environmental and host factors that contribute to prion strain evolution.Acta neuropathologica · 2021Review
- Efficient interspecies transmission of synthetic prions.PLoS pathogens · 2021Article
- Structurally distinct external solvent-exposed domains drive replication of major human prions.PLoS pathogens · 2021Article
- Allelic Interference in Prion Replication Is Modulated by the Convertibility of the Interfering PrPmBio · 2021Article
- Crossing Species Barriers Relies on Structurally Distinct Prion Assemblies and Their Complementation.Molecular neurobiology · 2020Article
- Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT-P301L mutation.Acta neuropathologica · 2020Article
- Chronic wasting disease (CWD) prion strains evolve via adaptive diversification of conformers in hosts expressing prion protein polymorphisms.The Journal of biological chemistry · 2020Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
The unique phenotypic characteristics of mammalian prions are thought to be encoded in the conformation of pathogenic prion proteins (PrP(Sc)). The molecular mechanism responsible for the adaptation, mutation, and evolution of prions observed in cloned cells and upon crossing the species barrier remains unsolved. Using biophysical techniques and conformation-dependent immunoassays in tandem, we isolated two distinct populations of PrP(Sc) particles with different conformational stabilities and aggregate sizes, which frequently co-exist in the most common human prion disease, sporadic Creutzfeldt-Jakob disease. The protein misfolding cyclic amplification replicates each of the PrP(Sc) particle types independently and leads to the competitive selection of those with lower initial conformational stability. In serial propagation with a nonglycosylated mutant PrP(C) substrate, the dominant PrP(Sc) conformers are subject to further evolution by natural selection of the subpopulation with the highest replication rate due to its lowest stability. Cumulatively, the data show that sporadic Creutzfeldt-Jakob disease PrP(Sc) is not a single conformational entity but a dynamic collection of two distinct populations of particles. This implies the co-existence of different prions, whose adaptation and evolution are governed by the selection of progressively less stable, faster replicating PrP(Sc) conformers.
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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.