Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The cerebrospinal fluid (CSF) real-time quaking-induced conversion assay (RT-QuIC) is an ultrasensitive prion amyloid seeding assay for diagnosis of sporadic Creutzfeldt-Jakob disease (CJD) but several prion strains remain unexplored or resistant to conversion with commonly used recombinant prion protein (rPrP) substrates. Here, bank vole (BV) rPrP was used to study seeding by a wide range of archived post-mortem human CSF samples from cases of sporadic, acquired and various inherited prion diseases in high throughput 384-well format. BV rPrP substrate yielded positive reactions in 70/79 cases of sporadic CJD [Sensitivity 88.6% (95% CI 79.5-94.7%)], 1/2 variant CJD samples, and 9/20 samples from various inherited prion diseases; 5/57 non-prion disease control CSFs had positive reactions, yielding an overall specificity of 91.2% (95% CI 80.1-97.1%). Despite limitations of using post-mortem samples and our results' discrepancy with other studies, we demonstrated for the first time that BV rPrP is susceptible to conversion by human CSF samples containing certain prion strains not previously responsive in conventional rPrPs, thus justifying further optimisation for wider diagnostic and prognostic use.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7933407 | PMC |
| http://dx.doi.org/10.1038/s41598-021-84527-9 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A model for propagation of RNA structural memory through biomolecular condensates.
Nat Cell Biol
August 2025
Molecular Medicine Program, Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT, USA.
We hypothesize that stress-induced RNA structural changes, stabilized by RNA-binding proteins in biomolecular condensates, propagate via conformational catalysis in a prion-like manner across generations. Our model suggests that RNA structure encodes heritable memory, and its roles should be explored in epigenetic inheritance, evolutionary adaptation and disease.
View Article and Find Full Text PDFInsights into the Diagnosis, Treatment, and Management of Prion Diseases.
CNS Neurol Disord Drug Targets
July 2025
Department of Pharmacy Practice, School of Pharmacy, IMU University, Kuala Lumpur, Malaysia.
The normal cellular prion protein (PrPC) can misfold into an infectious and pathogenic form (PrPSc) to produce prion diseases, also known as transmissible spongiform encephalopathies (TSEs), which are rare and deadly neurodegenerative conditions. The conversion of PrPC to PrPSc, which builds up as toxic aggregates in the central nervous system, is caused by sporadic, inherited, or acquired pathways. PrPSc-induced proteostasis failure, oxidative stress, neuronal toxicity, and progressive neurodegeneration are characteristics of pathogenesis.
View Article and Find Full Text PDFA review on current theories and potential therapies for prion diseases.
Mol Biol Rep
July 2025
Medical Bionanotechnology Lab, Department of Obstetrics and Gynaecology, Centre for Global Health Research, Saveetha Medical College, Saveetha Institute of Medical and Technical Sciences, Thandalam, Chennai, 602101, India.
Prion diseases are neurodegenerative disorders that affect both humans and animals. They are commonly characterized by the absence of DNA and RNA and are distinguished from inherited or infectious forms. The cellular prion proteins (PrP) misfold and accumulate into their pathogenic isoforms in these diseases.
View Article and Find Full Text PDFInherited prion disease caused by a novel frameshift mutation of resulting in protein truncation at codon 157.
J Alzheimers Dis
August 2025
MRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, London, UK.
BackgroundPrP systemic amyloidosis is increasingly recognized as a novel inherited prion disease (IPD) syndrome caused by C-terminal truncating mutations. As well as systemic manifestations they cause gradually progressive cognitive impairment with neurofibrillary tangle pathology which can be mistaken for Alzheimer's disease (AD).ObjectiveWe describe the clinical, biomarker and neuropathological features of a novel frameshift mutation of resulting in protein truncation at codon 157.
View Article and Find Full Text PDFDiverse effects of coexpression of human SOD1 variants on motor neuron disease.
Hum Mol Genet
August 2025
Department of Medical Biosciences, Umeå University, Umeå, SE 901 85, Sweden.
Mutations in superoxide dismutase-1 (SOD1) are a common cause of amyotrophic lateral sclerosis (ALS). Inheritance is as a rule dominant, but in carriers of the most common mutation, D90A, disease can develop in both homozygous and, more rarely, in heterozygous individuals with unexplained differences in clinical presentation. There is mounting evidence that prion-like spread of SOD1 aggregation is the primary cause of the disease.
View Article and Find Full Text PDF