ArticlemBio2013
Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification.
Article in mBio, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
40 citing papers in PubMed, 58 citations in OpenAlex.
- Effect of incineration, co-incineration and combustion on TSE hazards in category 1 animal by-products.EFSA journal. European Food Safety Authority · 2025Article
- Detection of prions in oocytes and ovaries of ewes naturally infected with classical scrapie.Veterinary research · 2025Article
- No evidence of subclinical infection in sheep surviving oral challenge with prions.The Journal of general virology · 2025Article
- Biological Fluid Biomarkers in Human Prion Diseases with a Note on Biosafety.Sub-cellular biochemistry · 2025Review
- Retention of prions in the polychaeteHeliyon · 2024Article
- Plants as vectors for environmental prion transmission.iScience · 2023Article
- PMCA screening of retropharyngeal lymph nodes in white-tailed deer and comparisons with ELISA and IHC.Scientific reports · 2023Article
- Conventional and State-of-the-Art Detection Methods of Bovine Spongiform Encephalopathy (BSE).International journal of molecular sciences · 2023Review
- Development of a sensitive real-time quaking-induced conversion (RT-QuIC) assay for application in prion-infected blood.PloS one · 2023Article
- Biodegradation of bovine spongiform encephalopathy prions in compost.Scientific reports · 2022Article
- Subclinical infection occurs frequently following low dose exposure to prions by blood transfusion.Scientific reports · 2022Article
- The importance of ongoing international surveillance for Creutzfeldt-Jakob disease.Nature reviews. Neurology · 2021Review
- White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains.Scientific reports · 2021Article
- Preclinical transmission of prions by blood transfusion is influenced by donor genotype and route of infection.PLoS pathogens · 2021Article
- Detection of Pathognomonic Biomarker PrPBiomolecules · 2020Review
- PMCA Applications for Prion Detection in Peripheral Tissues of Patients with Variant Creutzfeldt-Jakob Disease.Biomolecules · 2020Review
- Article
- Improving the Predictive Value of Prion Inactivation Validation Methods to Minimize the Risks of Iatrogenic Transmission With Medical Instruments.Frontiers in bioengineering and biotechnology · 2020Review
- Prion strain-dependent tropism is maintained between spleen and granuloma and relies on lymphofollicular structures.Scientific reports · 2019Article
- Thermostability as a highly dependent prion strain feature.Scientific reports · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Measurements of the presence of prions in biological tissues or fluids rely more and more on cell-free assays. Although protein misfolding cyclic amplification (PMCA) has emerged as a valuable, sensitive tool, it is currently hampered by its lack of robustness and rapidity for high-throughput purposes. Here, we made a number of improvements making it possible to amplify the maximum levels of scrapie prions in a single 48-h round and in a microplate format. The amplification rates and the infectious titer of the PMCA-formed prions appeared similar to those derived from the in vivo laboratory bioassays. This enhanced technique also amplified efficiently prions from different species, including those responsible for human variant Creutzfeldt-Jakob disease. This new format should help in developing ultrasensitive, high-throughput prion assays for cognitive, diagnostic, and therapeutic applications. IMPORTANCE The method developed here allows large-scale, fast, and reliable cell-free amplification of subinfectious levels of prions from different species. The sensitivity and rapidity achieved approach or equal those of other recently developed prion-seeded conversion assays. Our simplified assay may be amenable to high-throughput, automated purposes and serve in a complementary manner with other recently developed assays for urgently needed antemortem diagnostic tests, by using bodily fluids containing small amounts of prion infectivity. Such a combination of assays is of paramount importance to reduce the transfusion risk in the human population and to identify asymptomatic carriers of variant Creutzfeldt-Jakob disease.
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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.