Friday, March 23, 2012

Focus on Prions

New, Rapid, In-Vitro Prion Seeding Assay, RT-QuIC, Takes only Days instead of Months

Scientists from the Laboratory of Persistent Viral Diseases at Rocky Mountain Laboratories in Hamilton, Mont., and Japanese colleagues have developed a sensitive, rapid, and high-throughput assay for prion-seeding analysis on a BMG LABTECH microplate reader.  Using features found in the FLUOstar and POLARstar Omega microplate readers from BMG LABTECH, this new prion-seeding assay, Real-Time Quaking Induced Conversion assay (RT-QuIC), takes days to perform rather than months like the standard animal bioassay.  The underlying reaction blends aspects of 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 PrPc to a beta sheet-rich amyloid fibrillar form.  The RT-QuIC is as sensitive as the animal bioassay, but can be accomplished in two days or less.  This method has greatly aided the detection and diagnosis of Transmissible Spongiform Encephalopathy (TSE) diseases such as Creutzfeldt-Jakob disease in humans, scrapie in sheep, and chronic wasting disease in deer and elk.

To read the entire article, visit:

For more information on the Omega Series of Microplate Readers used in this study, visit:

1 comment:

  1. This is a fantastic new assay that will allow prion and prion-like diseases to be studied in the test tube (or microplate) rather than in the whole animal. Prior to this new test, drugs to inhibit prion aggregation took months to determine their effect. Now inhibition drugs can be screened in days, greatly speeding up the time to find possible cures to humans and to live stock.


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