ArticlePloS one2012
Detection of prion protein particles in blood plasma of scrapie infected sheep.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Analysis of Single Particles of Amyloid Beta and α-Synuclein With Seeded Amplification for the Diagnosis of Alzheimer's and Parkinson's Disease.Biotechnology and applied biochemistry · 2026Article
- Cerebrospinal Fluid and Plasma Small Extracellular Vesicles and miRNAs as Biomarkers for Prion Diseases.International journal of molecular sciences · 2021Article
- Classical scrapie in small ruminants is caused by at least four different prion strains.Veterinary research · 2021Article
- Detection of Pathognomonic Biomarker PrPBiomolecules · 2020Review
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- Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.Scientific reports · 2016Article
- Application of an Amyloid Beta Oligomer Standard in the sFIDA Assay.Frontiers in neuroscience · 2016Article
- Prenatal transmission of scrapie in sheep and goats: A case study for veterinary public health.Open veterinary journal · 2016Review
- Characterisation of the circulating acellular proteome of healthy sheep using LC-MS/MS-based proteomics analysis of serum.Proteome science · 2016Article
- Detection of cellular prion protein in exosomes derived from ovine plasma.The Journal of general virology · 2015Article
- Immediate and Ongoing Detection of Prions in the Blood of Hamsters and Deer following Oral, Nasal, or Blood Inoculations.Journal of virology · 2015Article
- Mechanism of scrapie prion precipitation with phosphotungstate anions.ACS chemical biology · 2015Article
- Classical natural ovine scrapie prions detected in practical volumes of blood by lamb and transgenic mouse bioassays.Journal of veterinary science · 2015Article
- First demonstration of transmissible spongiform encephalopathy-associated prion protein (PrPTSE) in extracellular vesicles from plasma of mice infected with mouse-adapted variant Creutzfeldt-Jakob disease by in vitro amplification.The Journal of biological chemistry · 2014Article
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- Accumulation profiles of PrP(Sc) in hemal nodes of naturally and experimentally scrapie-infected sheep.BMC veterinary research · 2013Article
- Identification of misfolded proteins in body fluids for the diagnosis of prion diseases.International journal of cell biology · 2013Review
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Corrections and comments
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
Abstract
Prion diseases are transmissible neurodegenerative diseases affecting humans and animals. The agent of the disease is the prion consisting mainly, if not solely, of a misfolded and aggregated isoform of the host-encoded prion protein (PrP). Transmission of prions can occur naturally but also accidentally, e.g. by blood transfusion, which has raised serious concerns about blood product safety and emphasized the need for a reliable diagnostic test. In this report we present a method based on surface-FIDA (fluorescence intensity distribution analysis), that exploits the high state of molecular aggregation of PrP as an unequivocal diagnostic marker of the disease, and show that it can detect infection in blood. To prepare PrP aggregates from blood plasma we introduced a detergent and lipase treatment to separate PrP from blood lipophilic components. Prion protein aggregates were subsequently precipitated by phosphotungstic acid, immobilized on a glass surface by covalently bound capture antibodies, and finally labeled with fluorescent antibody probes. Individual PrP aggregates were visualized by laser scanning microscopy where signal intensity was proportional to aggregate size. After signal processing to remove the background from low fluorescence particles, fluorescence intensities of all remaining PrP particles were summed. We detected PrP aggregates in plasma samples from six out of ten scrapie-positive sheep with no false positives from uninfected sheep. Applying simultaneous intensity and size discrimination, ten out of ten samples from scrapie sheep could be differentiated from uninfected sheep. The implications for ante mortem diagnosis of prion diseases are discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.