ArticleProceedings of the National Academy of Sciences of the United States of America2020
Highly infectious prions are not directly neurotoxic.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Intracellular trafficking SNARE protein, syntaxin-6, modifies prion cellular phenotypes and risk of disease development in vivo.Acta neuropathologica · 2025Article
- Human Genetic Evidence for New Targets in Prion Diseases: Opportunities and Challenges.Sub-cellular biochemistry · 2025Review
- "Proteinjury": a universal pathological mechanism mediated by cerebrospinal fluid in neurodegeneration and trauma.Frontiers in cell and developmental biology · 2025Review
- Single-cell transcriptomics unveils molecular signatures of neuronal vulnerability in a mouse model of prion disease that overlap with Alzheimer's disease.Nature communications · 2024Article
- Article
- Creutzfeldt-Jakob Disease and Fatal Familial Insomnia: Demographics and In-Hospital Mortality in Spain.Journal of clinical medicine · 2024Article
- Cleavage site-directed antibodies reveal the prion protein in humans is shed by ADAM10 at Y226 and associates with misfolded protein deposits in neurodegenerative diseases.Acta neuropathologica · 2024Article
- Review
- Efficient transmission of human prion diseases to a glycan-free prion protein-expressing host.Brain : a journal of neurology · 2024Article
- Article
- Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake.Journal of biochemistry · 2023Article
- Prion strains viewed through the lens of cryo-EM.Cell and tissue research · 2023Review
- Advanced Situation with Recombinant Toxins: Diversity, Production and Application Purposes.International journal of molecular sciences · 2023Review
- Essential Components of Synthetic Infectious Prion Formation De Novo.Biomolecules · 2022Review
- Microglia deficiency accelerates prion disease but does not enhance prion accumulation in the brain.Glia · 2022Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- A high-content neuron imaging assay demonstrates inhibition of prion disease-associated neurotoxicity by an anti-prion protein antibody.Scientific reports · 2022Article
- Neuroprotective effect and potential of cellular prion protein and its cleavage products for treatment of neurodegenerative disorders part I. a literature review.Expert review of neurotherapeutics · 2021Review
- C. elegans detects toxicity of traumatic brain injury generated tau.Neurobiology of disease · 2021Article
- The degree of astrocyte activation is predictive of the incubation time to prion disease.Acta neuropathologica communications · 2021Article
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
Prions are infectious agents which cause rapidly lethal neurodegenerative diseases in humans and animals following long, clinically silent incubation periods. They are composed of multichain assemblies of misfolded cellular prion protein. While it has long been assumed that prions are themselves neurotoxic, recent development of methods to obtain exceptionally pure prions from mouse brain with maintained strain characteristics, and in which defined structures-paired rod-like double helical fibers-can be definitively correlated with infectivity, allowed a direct test of this assertion. Here we report that while brain homogenates from symptomatic prion-infected mice are highly toxic to cultured neurons, exceptionally pure intact high-titer infectious prions are not directly neurotoxic. We further show that treatment of brain homogenates from prion-infected mice with sodium lauroylsarcosine destroys toxicity without diminishing infectivity. This is consistent with models in which prion propagation and toxicity can be mechanistically uncoupled.
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Registered trials
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