CSF PrP-amyloid seeding predicts clinical onset in inherited prion disease

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1. Très proche Données, outil ou méthode en commun Pas pertinent

   Recent advancements in QuIC-based diagnostic assays for sporadic and inherited prion diseases: focusing on the emerging role of ES-QuIC

   Rebecca Fox, Jennifer Myskiw, Ben A. Bailey-Elkin et al. · 2026 · Frontiers in Neuroscience · Pas encore résumé

   Cette revue présente les tests QuIC, notamment RT-QuIC, et un test modifié pour détecter les prions, tandis que l’article utilise RT-QuIC pour prédire la conversion clinique.

   Résumé scientifique

   Prion diseases are a group of fatal neurological disorders characterized by the accumulation of misfolded prion protein, primarily concentrated in the brain. The development of a family of assays known as Quaking-Induced Conversion (QuIC), particularly Real Time (RT)-QuIC, has revolutionized prion disease diagnosis by detecting and amplifying minute quantities of misfolded prion protein into measurable signals. Despite these advancements, certain prion subtypes, such as rare inherited forms or atypical sporadic variants, can produce structural configurations that resist amplification. To address these limitations, we developed a modified QuIC-based assay to increase sensitivity across a wide…

2. Proche Même méthode, autre problème Pas pertinent

   Cerebrospinal fluid α-synuclein seed amplification assay positivity identifies a prognostically distinct subgroup in amyotrophic lateral sclerosis

   Kazuhiro Obara, A. Mastrangelo, Agustina Ranieri et al. · 2026 · medRxiv · preprint, non relu par les pairs · Pas encore résumé

   Cette étude utilise un test d’amplification de graines α-synucléine dans le LCR pour définir un sous-groupe pronostique, tandis que l’article évalue RT-QuIC pour prédire la conversion prion.

   Résumé scientifique

   Background: -synuclein (Lewy body-type) co-pathology has been identified at autopsy in a subset of patients with amyotrophic lateral sclerosis (ALS). However, its prevalence and prognostic relevance in vivo remain poorly characterized. Methods: We analyzed baseline cerebrospinal fluid (CSF) -synuclein seed amplification assay (Syn SAA) status in 443 patients with ALS from two cohorts (Nagoya, Japan, n = 248; Bologna, Italy, n = 195). Samples were classified as strong-positive, weak-positive, or negative based on RT-QuIC reactivity across replicate wells, using the assay's established a priori criteria at initial and repeat testing; classifications were corroborated by quantitative kinetic pa…

3. Proche Même question Pas pertinent

   PRNP D178N-129MM prion disease: Creutzfeldt-Jakob disease-like cortical ribboning without prominent early insomnia

   Wan-Yi Wei, Hai-Tian Nan, Zhong-Yun Chen et al. · 2026 · Frontiers in Neuroscience · Pas encore résumé

   Ce cas décrit une maladie à prions liée à PRNP et rapporte un RT-QuIC positif, tandis que l’article étudie le signal RT-QuIC chez des porteurs avant les symptômes.

   Résumé scientifique

   Background The PRNP p.Asp178Asn (D178N) mutation on a methionine-bearing codon-129 allele is classically associated with fatal familial insomnia (FFI), but some carriers develop a Creutzfeldt-Jakob disease (CJD)-like phenotype. Case presentation and findings We report a 59-year-old woman with two months of rapidly progressive cognitive-language decline, caregiver-observed nocturnal sitting-up and sleep talking, weight loss, extensive cortical diffusion-weighted imaging (DWI) ribboning, positive cerebrospinal fluid 14–3-3, and positive multisite skin real-time quaking-induced conversion. Electroencephalography showed diffuse slowing without periodic sharp-wave complexes. PRNP sequencing ident…

4. Proche Contexte plus large Pas pertinent

   Prevention of prion disease symptoms in mice with deep PrP lowering

   J. E. Gentile, J. E. Farley, M. N. Kelemen et al. · 2026 · bioRxiv preprint · Résumé IA disponible

   Cette étude teste chez la souris une thérapie abaissant PrP pour prévenir les symptômes, tandis que l’article examine un biomarqueur de conversion clinique chez des porteurs humains.

   En bref

   Chez la souris infectée par des prions, une forte réduction de PrP par siRNA maintient les animaux traités précocement sans symptômes jusqu’à 500 jours après inoculation.

5. Proche Contexte plus large Pas pertinent

   Reduced phosphatases and hyperphosphorylated glutamatergic receptors persist from early to late stages of prion disease

   Alexander J. Rajic, Daniel Ojeda-Juarez, Dipannita Sarkar et al. · 2026 · bioRxiv · preprint, non relu par les pairs · Pas encore résumé

   Cette étude suit les changements synaptiques et moléculaires chez des souris infectées par des prions, tandis que l’article suit l’ensemencement PrP dans le LCR de porteurs humains.

   Résumé scientifique

   Synapse loss occurs early in prion disease, yet the intracellular signaling driving this dysregulation remains poorly understood. Evidence of neuronal hyperactivity was reported in humans with sporadic and familial CJD as well as in the early stages of prion disease in mice (strain 22L). Here we perform a time course study of prion-infected mice (strain RML) and show an increase in the immediate-early gene, Arc, suggesting this is a conserved response to prions. We also observed a persistent decrease in phosphatase abundance (PP1α and PP2B) in the cerebral cortex starting at the earliest timepoint (preclinical). At this stage, mGluR5 dimers and phosphorylated AMPA receptors were increased. B…

6. Proche Contexte plus large Pas pertinent

   Cellular prion protein levels modulate nigrostriatal vulnerability to α-synuclein oligomers in Parkinson’s disease

   Flavio de Souza Júnyor, F. Leser, Sarah de Souza Albuquerque et al. · 2026 · Frontiers in Neuroscience · Pas encore résumé

   Cette étude examine le rôle de PrP dans la neurodégénérescence induite par α-synucléine dans la maladie de Parkinson, plutôt que la conversion clinique d’une maladie à prions.

   Résumé scientifique

   α-Synuclein oligomer (αSynO)-mediated neurodegeneration is a hallmark of Parkinson’s disease (PD) pathogenesis, yet the molecular mechanisms mediating this toxicity remain elusive. In this study, we investigated the cellular prion protein (PrPC) as a key modulator of αSynO-induced neurodegeneration using an integrative translational approach combining human transcriptomic analysis with in vivo bidirectional genetic modulation in mice. Bioinformatics analysis of postmortem substantia nigra samples revealed that the PRNP gene is significantly upregulated in idiopathic PD patients, with its co-expression network enriched for plasma membrane raft organization and synaptic vesicle dynamics. Singl…

7. Proche Même méthode, autre problème Pas pertinent

   α-Synuclein Seed Amplification Status Modifies the Relationship Between Plasma p-tau217, Amyloid and Fibrillar Tau

   Í. Rodríguez-Baz, Rosa Ferrer, M. Falip et al. · 2026 · Research Square · preprint, non relu par les pairs · Pas encore résumé

   Cette étude utilise un test d’amplification de graines α-synucléine dans le LCR et relie son statut à des biomarqueurs, tandis que l’article relie RT-QuIC à la conversion clinique.

   Résumé scientifique

   Abstract Background. Plasma p-tau217 is sufficient to establish a biological diagnosis of Alzheimer's disease (AD) and is and is increasingly used as a routine diagnostic tool. Many patients with AD also carry α-synuclein pathology, detectable by cerebrospinal fluid (CSF) seed amplification assay (αSynSAA). Seeding activity has been linked to more fibrillar tau than amyloid burden alone would predict, but whether this influences plasma p-tau217 levels, or compromises classification at clinical thresholds, is unknown. Methods. Cross-sectional analysis of the Alzheimer's Disease Neuroimaging Initiative. Plasma p-tau217 (Fujirebio Lumipulse) was compared by αSynSAA status conditional on amyloid…

8. Proche Même méthode, autre problème Pas pertinent

   Urine-Derived Neuronal Extracellular Vesicle α-Synuclein Seed Amplification Assay for Synucleinopathies: A Non-Invasive Biomarker Study.

   H. Tran, Huu Dat Nguyen, T. Nguyen et al. · 2026 · Movement Disorders · Pas encore résumé

   Cette étude applique RT-QuIC à des vésicules neuronales urinaires pour détecter l’α-synucléine, tandis que l’article l’applique au LCR pour prévoir la maladie à prions.

   Résumé scientifique

   BACKGROUND α-Synuclein aggregation is a pathological hallmark of synucleinopathies, including Parkinson's disease (PD) and multiple system atrophy (MSA). Although pathogenic α-synuclein seeds can be detected by real-time quaking-induced conversion (RT-QuIC), current assays primarily rely on cerebrospinal fluid, whose invasiveness limits repeated and large-scale applications. We therefore evaluated the feasibility of detecting pathogenic α-synuclein using urine-derived neuronal extracellular vesicles (NEVs). METHODS Urine-derived NEVs were enriched by direct immunoprecipitation using L1CAM-conjugated magnetic beads. The RT-QuIC assay was performed in 26 patients with PD, 13 with MSA, and 25 d…