ArticlePloS one2010
Sulfated dextrans enhance in vitro amplification of bovine spongiform encephalopathy PrP(Sc) and enable ultrasensitive detection of bovine PrP(Sc).
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 56 citations in OpenAlex.
- Evidence for multiple prion conformers in natural scrapie isolates.PLoS pathogens · 2026Article
- Administration of L-Type Bovine Spongiform Encephalopathy to Macaques to Evaluate Zoonotic Potential.Emerging infectious diseases · 2025Article
- Conventional and State-of-the-Art Detection Methods of Bovine Spongiform Encephalopathy (BSE).International journal of molecular sciences · 2023Review
- PMCA for ultrasensitive detection of prions and to study disease biology.Cell and tissue research · 2023Review
- Biodegradation of bovine spongiform encephalopathy prions in compost.Scientific reports · 2022Article
- Detection of Pathognomonic Biomarker PrPBiomolecules · 2020Review
- Bovine Spongiform Encephalopathy - A Review from the Perspective of Food Safety.Food safety (Tokyo, Japan) · 2019Review
- Modified Protein Misfolding Cyclic Amplification Overcomes Real-Time Quaking-Induced Conversion Assay Inhibitors in Deer Saliva To Detect Chronic Wasting Disease Prions.Journal of clinical microbiology · 2018Article
- Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells.Journal of virology · 2017Article
- PrP Knockout Cells Expressing Transmembrane PrP Resist Prion Infection.Journal of virology · 2017Article
- Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.Scientific reports · 2016Article
- Detection of Atypical H-Type Bovine Spongiform Encephalopathy and Discrimination of Bovine Prion Strains by Real-Time Quaking-Induced Conversion.Journal of clinical microbiology · 2016Article
- Article
- Heparin binding confers prion stability and impairs its aggregation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Article
- Rapid assessment of bovine spongiform encephalopathy prion inactivation by heat treatment in yellow grease produced in the industrial manufacturing process of meat and bone meals.BMC veterinary research · 2013Article
- Cellular aspects of prion replication in vitro.Viruses · 2013Review
- Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.International journal of cell biology · 2013Review
- Article
- Identification of misfolded proteins in body fluids for the diagnosis of prion diseases.International journal of cell biology · 2013Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPrions, infectious agents associated with prion diseases such as Creutzfeldt-Jakob disease in humans, bovine spongiform encephalopathy (BSE) in cattle, and scrapie in sheep and goats, are primarily comprised of PrP(Sc), a protease-resistant misfolded isoform of the cellular prion protein PrP(C). Protein misfolding cyclic amplification (PMCA) is a highly sensitive technique used to detect minute amounts of scrapie PrP(Sc). However, the current PMCA technique has been unsuccessful in achieving good amplification in cattle. The detailed distribution of PrP(Sc) in BSE-affected cattle therefore remains unknown. METHODOLOGY/PRINCIPAL
findingsWe report here that PrP(Sc) derived from BSE-affected cattle can be amplified ultra-efficiently by PMCA in the presence of sulfated dextran compounds. This method is capable of amplifying very small amounts of PrP(Sc) from the saliva, palatine tonsils, lymph nodes, ileocecal region, and muscular tissues of BSE-affected cattle. Individual differences in the distribution of PrP(Sc) in spleen and cerebrospinal fluid samples were observed in terminal-stage animals. However, the presence of PrP(Sc) in blood was not substantiated in the BSE-affected cattle examined. CONCLUSIONS/SIGNIFICANCE: The distribution of PrP(Sc) is not restricted to the nervous system and can spread to peripheral tissues in the terminal disease stage. The finding that PrP(Sc) could be amplified in the saliva of an asymptomatic animal suggests a potential usefulness of this technique for BSE diagnosis. This highly sensitive method also has other practical applications, including safety evaluation or safety assurance of products and byproducts manufactured from bovine source materials.
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