ArticleProtein science : a publication of the Protein Society2005
Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 93 citations in OpenAlex.
- Mechanistic Insights Behind the Self-Assembly of Human Insulin under the Influence of Surface-Engineered Gold Nanoparticles.ACS chemical neuroscience · 2024Article
- The Effect of Octapeptide Repeats on Prion Folding and Misfolding.International journal of molecular sciences · 2021Article
- The Nuclear Lamina: Protein Accumulation and Disease.Biomedicines · 2020Review
- Modeling PrPFrontiers in bioengineering and biotechnology · 2020Article
- 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
- Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis.Biophysical journal · 2018Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome.Scientific reports · 2017Article
- Purification and Fibrillation of Full-Length Recombinant PrP.Methods in molecular biology (Clifton, N.J.) · 2017Article
- The diversity and relationship of prion protein self-replicating states.Virus research · 2015Review
- Synthetic Aβ peptides acquire prion-like properties in the brain.Oncotarget · 2015Article
- Elongation of mouse prion protein amyloid-like fibrils: effect of temperature and denaturant concentration.PloS one · 2014Article
- Liberation of GPI-anchored prion from phospholipids accelerates amyloidogenic conversion.International journal of molecular sciences · 2013Article
- Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity.PloS one · 2013Article
- Amyloid core formed of full-length recombinant mouse prion protein involves sequence 127-143 but not sequence 107-126.PloS one · 2013Article
- A new mechanism for transmissible prion diseases.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- High pressure, a tool to switch between soluble and fibrillar prion protein structures.Communicative & integrative biology · 2012Article
- Article
- Role of prion protein aggregation in neurotoxicity.International journal of molecular sciences · 2012Review
- Purification and fibrillation of full-length recombinant PrP.Methods in molecular biology (Clifton, N.J.) · 2012Article
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5 authors at 3 institutions in 2 countries.
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Abstract
In recent studies, the amyloid form of recombinant prion protein (PrP) encompassing residues 89-230 (rPrP 89-230) produced in vitro induced transmissible prion disease in mice. These studies showed that unlike "classical" PrP(Sc) produced in vivo, the amyloid fibrils generated in vitro were more proteinase-K sensitive. Here we demonstrate that the amyloid form contains a proteinase K-resistant core composed only of residues 152/153-230 and 162-230. The PK-resistant fragments of the amyloid form are similar to those observed upon PK digestion of a minor subpopulation of PrP(Sc) recently identified in patients with sporadic Creutzfeldt-Jakob disease (CJD). Remarkably, this core is sufficient for self-propagating activity in vitro and preserves a beta-sheet-rich fibrillar structure. Full-length recombinant PrP 23-230, however, generates two subpopulations of amyloid in vitro: One is similar to the minor subpopulation of PrP(Sc), and the other to classical PrP(Sc). Since no cellular factors or templates were used for generation of the amyloid fibrils in vitro, we speculate that formation of the subpopulation of PrP(Sc) with a short PK-resistant C-terminal region reflects an intrinsic property of PrP rather than the influence of cellular environments and/or cofactors. Our work significantly increases our understanding of the biochemical nature of prion infectious agents and provides a fundamental insight into the mechanisms of prions biogenesis.
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