ArticleProceedings of the National Academy of Sciences of the United States of America2007
Accumulation of prion protein in the brain that is not associated with transmissible disease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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Who cites it
92 citing papers in PubMed, 180 citations in OpenAlex.
- The L108I polymorphism in mouse prion protein drives spontaneous disease and enhances transmission of atypical and classical prion strains.Brain pathology (Zurich, Switzerland) · 2026Article
- Disease-Associated Q159X Mutant Prion Protein Is Sufficient to Cause Fatal Degenerative Disease in Mice.Molecular neurobiology · 2024Article
- Creutzfeldt-Jakob Disease and Fatal Familial Insomnia: Demographics and In-Hospital Mortality in Spain.Journal of clinical medicine · 2024Article
- Prion strains viewed through the lens of cryo-EM.Cell and tissue research · 2023Review
- The manifold role of octapeptide repeats in prion protein assembly.Peptide science (Hoboken, N.J.) · 2023Article
- Subclinical infection occurs frequently following low dose exposure to prions by blood transfusion.Scientific reports · 2022Article
- The protean prion protein.PLoS biology · 2020Article
- Spontaneous generation of prions and transmissible PrP amyloid in a humanised transgenic mouse model of A117V GSS.PLoS biology · 2020Article
- PrPSc with Seeding Activity Extensively Overlaps with Proteinase-Resistant PrPSc Rather than Infectious PrPSc.Pathogens (Basel, Switzerland) · 2020Article
- Understanding Prion Strains: Evidence from Studies of the Disease Forms Affecting Humans.Viruses · 2019Review
- Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro.Scientific reports · 2019Article
- Two distinct prions in fatal familial insomnia and its sporadic form.Brain communications · 2019Article
- Variable Protease-Sensitive Prionopathy Transmission to Bank Voles.Emerging infectious diseases · 2019Article
- Recent Advances in Understanding Mammalian Prion Structure: A Mini Review.Frontiers in molecular neuroscience · 2019Article
- Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases.Nature neuroscience · 2018Review
- Lysosomal Quality Control in Prion Diseases.Molecular neurobiology · 2018Review
- PrP P102L and Nearby Lysine Mutations Promote SpontaneousJournal of virology · 2017Article
- Mitochondrial Respiration Is Impaired during Late-Stage Hamster Prion Infection.Journal of virology · 2017Article
- Activation of microglia by retroviral infection correlates with transient clearance of prions from the brain but does not change incubation time.Brain pathology (Zurich, Switzerland) · 2017Article
- Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity.PLoS pathogens · 2017Article
32 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Prion diseases or transmissible spongiform encephalopathies are characterized histopathologically by the accumulation of prion protein (PrP) ranging from diffuse deposits to amyloid plaques. Moreover, pathologic PrP isoforms (PrP(Sc)) are detected by immunoblot analysis and used both as diagnostic markers of disease and as indicators of the presence of infectivity in tissues. It is not known which forms of PrP are associated with infectivity. To address this question, we performed bioassays using human brain extracts from two cases with phenotypically distinct forms of familial prion disease (Gerstmann-Sträussler-Scheinker P102L). Both cases had PrP accumulations in the brain, but each had different PrP(Sc) isoforms. Only one of the brains had spongiform degeneration. Tissue from this case transmitted disease efficiently to transgenic mice (Tg PrP101LL), resulting in spongiform encephalopathy. In contrast, inoculation of tissue from the case with no spongiform degeneration resulted in almost complete absence of disease transmission but elicited striking PrP-amyloid deposition in several recipient mouse brains. Brains of these mice failed to transmit any neurological disease on passage, but PrP-amyloid deposition was again observed in the brains of recipient mice. These data suggest the possible isolation of an infectious agent that promotes PrP amyloidogenesis in the absence of a spongiform encephalopathy. Alternatively, the infectious agent may be rendered nonpathogenic by sequestration in amyloid plaques, or PrP amyloid can seed amyloid accumulation in the brain, causing a proteinopathy that is unrelated to prion disease. Formation of PrP amyloid may therefore not necessarily be a reliable marker of transmissible spongiform encephalopathy infectivity.
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