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Rapid End-Point Quantitation of Prion Seeding Activity with Sensitivity Comparable to Bioassays

PLoS Pathogens · 2010 · Vol. 6(12) · pp. e1001217–e1001217
Jason M. WilhamChristina D. OrrúRichard A. BessenRyuichiro AtarashiKazunori SanoBrent RaceKimberly Meade‐WhiteLara M. TaubnerAndrew TimmesByron Caughey

Abstract

A major problem for the effective diagnosis and management of prion diseases is the lack of rapid high-throughput assays to measure low levels of prions. Such measurements have typically required prolonged bioassays in animals. Highly sensitive, but generally non-quantitative, prion detection methods have been developed based on prions' ability to seed the conversion of normally soluble protease-sensitive forms of prion protein to protease-resistant and/or amyloid fibrillar forms. Here we describe an approach for estimating the relative amount of prions using a new prion seeding assay called real-time quaking induced conversion assay (RT-QuIC). The underlying reaction blends aspects of the previously described quaking-induced conversion (QuIC) and amyloid seeding assay (ASA) methods and involves prion-seeded conversion of the alpha helix-rich form of bacterially expressed recombinant PrP(C) to a beta sheet-rich amyloid fibrillar form. The RT-QuIC is as sensitive as the animal bioassay, but can be accomplished in 2 days or less. Analogous to end-point dilution animal bioassays, this approach involves testing of serial dilutions of samples and statistically estimating the seeding dose (SD) giving positive responses in 50% of replicate reactions (SD(50)). Brain tissue from 263K scrapie-affected hamsters gave SD(50) values of 10(11)-10(12)/g, making the RT-QuIC similar in sensitivity to end-point dilution bioassays. Analysis of bioassay-positive nasal lavages from hamsters affected with transmissible mink encephalopathy gave SD(50) values of 10(3.5)-10(5.7)/ml, showing that nasal cavities release substantial prion infectivity that can be rapidly detected. Cerebral spinal fluid from 263K scrapie-affected hamsters contained prion SD(50) values of 10(2.0)-10(2.9)/ml. RT-QuIC assay also discriminated deer chronic wasting disease and sheep scrapie brain samples from normal control samples. In principle, end-point dilution quantitation can be applied to many types of prion and amyloid seeding assays. End point dilution RT-QuIC provides a sensitive, rapid, quantitative, and high throughput assay of prion seeding activity.

Prion Diseases and Protein MisfoldingBioassaySerial dilutionScrapieRecombinant DNAAmyloid (mycology)BiologySeedingProteinase KMolecular biologyChemistry

MeSH terms

AmyloidAnimalsBrainCerebrospinal FluidDeerCricetinaeHumansMethodsMinkPrionsSheepProtein Structure, SecondaryEndpoint DeterminationHigh-Throughput Screening Assays

Funding

  • National Institutes of Health
  • National Institute of Allergy and Infectious Diseases
Citations
503
FWCI
7.30
field-weighted impact
References
51
Percentile
98%
vs. same field & year
Citations per year
References
A SIMPLE METHOD OF ESTIMATING FIFTY PER CENT ENDPOINTS12
American Journal of Epidemiology · 1938 · 20,055 citations
A simple method of estimating 50 per cent end points
Medical Entomology and Zoology · 1938 · 8,379 citations
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