ArticleActa neuropathologica2022
Cryo-EM structures of prion protein filaments from Gerstmann-Sträussler-Scheinker disease.
Article in Acta neuropathologica, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 72 citations in OpenAlex.
- Distinctive properties of the prion protein in the brain and retina in the amyloidosis associated with the PRNP F198S mutation.Acta neuropathologica · 2026Article
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- Article
- Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathway.Nature communications · 2026Article
- Distinctive properties of the prion protein in the brain and retina in the amyloidosis associated with the PRNP F198S Mutation.Research square · 2026Article
- Rapid generation of prion disease models using AAV-delivered PrP variants in knockout mice.Brain pathology (Zurich, Switzerland) · 2026Article
- A model-based prion vaccine protects a transgenic mouse line carrying a Gerstmann-Sträussler-Scheinker disease mutation.Acta neuropathologica · 2026Article
- Plasmonics-Enhanced Characterization of Cervid PrP (87-114) Fragment Aggregates in Solution.Journal of biophotonics · 2026Article
- 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
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Regulated coexpression of PrP from different species in mice impacts the replication and host range properties of prion strains.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and cellular properties of human prion protein oligomers.Communications biology · 2025Article
- A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Celebrating neuropathology's contributions to Alzheimer's Disease Research Centers.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Evidence of a novel α-synuclein strain isolated from a Parkinson's disease with dementia patient sample.Acta neuropathologica communications · 2025Article
- Variably protease-sensitive prionopathy: mass spectrometry analysis of the pathogenic prion protein provides a new perspective.Acta neuropathologica communications · 2025Article
- Advances in the Study of Protein Deamidation: Unveiling Its Influence on Aging, Disease Progression, Forensics and Therapeutic Efficacy.Proteomes · 2025Review
- Cryo-EM evidence for a common factor in Alzheimer's and other neurodegenerations.bioRxiv : the preprint server for biology · 2025Article
- PRNP E146G mutation inherited prion disease: distinctive clinical, pathological and fluid biomarker features.Journal of neurology · 2025Article
- Limitations and Applications of Rodent Models in Tauopathy and Synucleinopathy Research.Journal of neurochemistry · 2025Review
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15 authors at 2 institutions in 1 country.
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Abstract
Prion protein (PrP) aggregation and formation of PrP amyloid (APrP) are central events in the pathogenesis of prion diseases. In the dominantly inherited prion protein amyloidosis known as Gerstmann-Sträussler-Scheinker (GSS) disease, plaques made of PrP amyloid are present throughout the brain. The c.593t > c mutation in the prion protein gene (PRNP) results in a phenylalanine to serine amino acid substitution at PrP residue 198 (F198S) and causes the most severe amyloidosis among GSS variants. It has been shown that neurodegeneration in this disease is associated with the presence of extracellular APrP plaques and neuronal intracytoplasmic Tau inclusions, that have been shown to contain paired helical filaments identical to those found in Alzheimer disease. Using cryogenic electron microscopy (cryo-EM), we determined for the first time the structures of filaments of human APrP, isolated post-mortem from the brain of two symptomatic PRNP F198S mutation carriers. We report that in GSS (F198S) APrP filaments are composed of dimeric, trimeric and tetrameric left-handed protofilaments with their protomers sharing a common protein fold. The protomers in the cross-β spines consist of 62 amino acids and span from glycine 80 to phenylalanine 141, adopting a previously unseen spiral fold with a thicker outer layer and a thinner inner layer. Each protomer comprises nine short β-strands, with the β1 and β8 strands, as well as the β4 and β9 strands, forming a steric zipper. The data obtained by cryo-EM provide insights into the structural complexity of the PrP filament in a dominantly inherited human PrP amyloidosis. The novel findings highlight the urgency of extending our knowledge of the filaments' structures that may underlie distinct clinical and pathologic phenotypes of human neurodegenerative diseases.
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