ArticleThe Journal of biological chemistry2013
Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.
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 40 papers.
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Who cites it
40 citing papers in PubMed.
- Overexpression of bank vole PrP(I109) in mice induces a spontaneous atypical prion disease with sex-dependent onset, early NfL elevation, and universal prion strain permissiveness.Acta neuropathologica communications · 2026Article
- Reactive Microglia and Astrocytes as Therapeutic Targets in Prion Diseases.Sub-cellular biochemistry · 2025Review
- Biological Fluid Biomarkers in Human Prion Diseases with a Note on Biosafety.Sub-cellular biochemistry · 2025Review
- Multiple steps of prion strain adaptation to a new host.Frontiers in neuroscience · 2024Article
- Role of sialylation of N-linked glycans in prion pathogenesis.Cell and tissue research · 2023Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Overexpression of mouse prion protein in transgenic mice causes a non-transmissible spongiform encephalopathy.Scientific reports · 2022Article
- Asymmetric-flow field-flow fractionation of prions reveals a strain-specific continuum of quaternary structures with protease resistance developing at a hydrodynamic radius of 15 nm.PLoS pathogens · 2021Article
- From Posttranslational Modifications to Disease Phenotype: A Substrate Selection Hypothesis in Neurodegenerative Diseases.International journal of molecular sciences · 2021Review
- Understanding Intra-Species and Inter-Species Prion Conversion and Zoonotic Potential Using Protein Misfolding Cyclic Amplification.Frontiers in aging neuroscience · 2021Review
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Cofactor and glycosylation preferences for in vitro prion conversion are predominantly determined by strain conformation.PLoS pathogens · 2020Article
- Underglycosylated prion protein modulates plaque formation in the brain.The Journal of clinical investigation · 2020Article
- Role of prion protein glycosylation in replication of human prions by protein misfolding cyclic amplification.Laboratory investigation; a journal of technical methods and pathology · 2019Article
- Synthetic Prion Selection and Adaptation.Molecular neurobiology · 2019Article
- Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology.Viruses · 2018Review
- Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Molecular psychiatry · 2018Article
- Analysis of Covalent Modifications of Amyloidogenic Proteins Using Two-Dimensional Electrophoresis: Prion Protein and Its Sialylation.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
With the development of protein misfolding cyclic amplification (PMCA), the topic of faithful propagation of prion strain-specific structures has been constantly debated. Here we show that by subjecting brain material of a synthetic strain consisting of a mixture of self-replicating states to PMCAb, selective amplification of PrP(Sc) could be achieved, and that PMCAb mimicked the evolutionary trend observed during serial transmission in animals. On the other hand, using modified PMCAb conditions that employ partially deglycosylated PrP(C) (dgPMCAb), an alternative transmissible state referred to as atypical protease-resistant form of the prion protein (atypical PrPres) was selectively amplified from a mixture. Surprisingly, when hamster-adapted strains (263K and Hyper) were subjected to dgPMCAb, their proteinase K digestion profile underwent a dramatic transformation, suggesting that a mixture of atypical PrPres and PrP(Sc) might be present in brain-derived materials. However, detailed analysis revealed that the proteinase K-resistant profile of PrP(Sc) changed in response to dgPMCAb. Despite these changes, the 263K strain-specific disease phenotype was preserved after passage through dgPMCAb. This study revealed that the change in PrP(Sc) biochemical phenotype does not always represent an irreversible transformation of a strain, but rather demonstrated the existence of a wide range of variation for strain-specific physical features in response to a change in prion replication environment. The current work introduced a new PMCA technique for amplification of atypical PrPres and raised a number of questions about the need for a clever distinction between actual strain mutation and variation of strain-specific features in response to a change in the replication environment.
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