ArticleActa neuropathologica communications2013
Establishing quantitative real-time quaking-induced conversion (qRT-QuIC) for highly sensitive detection and quantification of PrPSc in prion-infected tissues.
Article in Acta neuropathologica communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Novel Prion Protein Gene (bioRxiv : the preprint server for biology · 2026Article
- Identification and initial characterization of novel prion protein gene (Frontiers in veterinary science · 2026Article
- A quantitative Lewy-fold-specific alpha-synuclein seed amplification assay as a progression marker for Parkinson's disease.Acta neuropathologica · 2025Article
- Prion diseases disrupt glutamate/glutamine metabolism in skeletal muscle.PLoS pathogens · 2024Article
- Enhanced quantitation of pathological α-synuclein in patient biospecimens by RT-QuIC seed amplification assays.PLoS pathogens · 2024Article
- Prion Seeding Activity in Plant Tissues Detected by RT-QuIC.Pathogens (Basel, Switzerland) · 2024Article
- Sensitive detection of pathological seeds of α-synuclein, tau and prion protein on solid surfaces.PLoS pathogens · 2024Article
- Detection of skin α-synuclein using RT-QuIC as a diagnostic biomarker for Parkinson's disease in the Chinese population.European journal of medical research · 2024Article
- Clinical biomarkers for Lewy body diseases.Cell & bioscience · 2023Review
- Conventional and State-of-the-Art Detection Methods of Bovine Spongiform Encephalopathy (BSE).International journal of molecular sciences · 2023Review
- A review of the current research on in vivo and in vitro detection for alpha-synuclein: a biomarker of Parkinson's disease.Analytical and bioanalytical chemistry · 2023Review
- An arrayed genome-wide perturbation screen identifies the ribonucleoprotein Hnrnpk as rate-limiting for prion propagation.The EMBO journal · 2022Article
- The Future of Seed Amplification Assays and Clinical Trials.Frontiers in aging neuroscience · 2022Review
- Bank vole prion protein extends the use of RT-QuIC assays to detect prions in a range of inherited prion diseases.Scientific reports · 2021Article
- Quaternary Structure Changes for PrPMolecular neurobiology · 2021Article
- Potential sources of interference with the highly sensitive detection and quantification of alpha-synuclein seeds by qRT-QuIC.FEBS open bio · 2020Article
- A Case of a Patient Who Presented with Rapidly Progressive Dementia and Capricious RT-QuIC Results.Dementia and neurocognitive disorders · 2020Article
- Postmortem Quantitative Analysis of Prion Seeding Activity in the Digestive System.Molecules (Basel, Switzerland) · 2019Article
- Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases.Molecular neurobiology · 2018Review
- Solvation-Guided Design of Fluorescent Probes for Discrimination of Amyloids.Scientific reports · 2018Article
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4 authors.
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Abstract
backgroundPrPSc, the only known constituent of prions, the infectious agents causing prion diseases, can be detected by real-time quaking-induced conversion (RT-QuIC). However, there is no efficient method to quantify the amount of PrPSc by RT-QuIC.
resultsHere we introduce quantitative RT-QuIC (qRT-QuIC) to quantify with high accuracy minute amounts of PrPSc in the brain and various peripheral tissues at levels far below detection by in vivo transmission. PrPSc is relatively resistant to treatment with proteinase K (PK). However, as there can also be a fraction of pathological PrP that is digested by PK, we use the term PrP27-30 to denote to the amount of PrPSc that can be detected by immunoblot after PK treatment. qRT-QuIC is based upon the quantitative correlation between the seeded amount of PrP27-30 and the lag time to the start of the conversion reaction detected by RT-QuIC. By seeding known amounts of PrP27-30 quantified by immunoblot into qRT-QuIC a standard calibration curve can be obtained. Based on this calibration curve, seeded undetermined amounts of PrP27-30 can be directly calculated. qRT-QuIC allowed to quantify PrP27-30 concentrations at extremely low levels as low as 10-15.5 g PrP27-30, which corresponds to 0.001 LD50 units obtained by in vivo i.c. transmission studies. We find that PrP27-30 concentration increases steadily in the brain after inoculation and can be detected at various time points during the incubation period in peripheral organs (spleen, heart, muscle, liver, kidney) in two experimental scrapie strains (RML, ME7) in the mouse.
conclusionsWe suggest that an automatic quantitative system to measure disease progression as well as prion contamination of organs, blood and food product is feasible. Moreover, the concept of qRT-QuIC should be applicable to measure other disease-associated proteins rich in β-pleated structures (amyloid) that bind ThT and that show seeded aggregation.
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