Prions are transmittable pathogens that cause an abnormal folding of a brain protein in both humans and animals. Infection results in brain damage and is fatal. Some examples of these neurodegenerative diseases are Bovine Spongiform Encephalopathy (Mad Cow Disease), Scrapie, Chronic Wasting Disease, and Creutzfeldt-Jakob Disease1
Previously, prions were studied using lengthy bioassays where infected animals were studied over long periods of time (1–6 months). This was both time consuming and costly to maintain the infected animal. Researchers at Rocky Mountain Laboratories in Hamilton, Montana, have developed a new prion seeding assay called Real-Time Quaking Induced Conversion Assay (RT-QuIC) that gives end point quantitation for measuring the levels of prions in infected samples2. This assay is both faster and higher throughput compared to previous methods. The assay can be completed in as short as 20 hours and is as sensitive, if not more so, than whole animal models.
German engineered for durability, BMG LABTECH’s Omega series of microplate readers have the ability to vigorously shake (700 rpm) and incubate microplates over long periods of time. A POLARstar Omega was used to measure RT-QuIC samples every 15 minutes for 20–68 hours while alternately shaking for a minute and resting for a minute.