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Related Experiment Video

Updated: May 24, 2026

Real-time Quaking-induced Conversion Assay for Detection of CWD Prions in Fecal Material
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New generation QuIC assays for prion seeding activity.

Christina D Orrù1, Jason M Wilham, Sarah Vascellari

  • 1Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, USA.

Prion
|March 17, 2012
PubMed
Summary

Abnormal prion proteins (PrP) can seed amyloid formation, enabling sensitive prion disease detection. Recent real-time quaking-induced conversion (RT-QuIC) assay improvements enhance detection in challenging samples like blood plasma.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Medical Diagnostics

Background:

  • Prion diseases are characterized by abnormal prion protein (PrP) forming amyloid fibrils.
  • The seeding ability of abnormal PrP is the basis for sensitive prion disease diagnostic assays.
  • Existing assays include rPrP-PMCA, S-QuIC, ASA, RT-QuIC, and eQuIC.

Purpose of the Study:

  • To summarize recent advancements in real-time quaking-induced conversion (RT-QuIC) assays.
  • To highlight improvements enhancing assay practicality, sensitivity, and quantitative capabilities.
  • To promote prion seeding activity detection in challenging biological fluids.

Main Methods:

  • Utilizing recombinant PrP(Sen) as a substrate for amyloid fibril formation.
  • Employing various QuIC assay formats, with a focus on RT-QuIC.

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Last Updated: May 24, 2026

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  • Summarizing modifications to RT-QuIC for improved performance.

    • Main Results:

    • Recent RT-QuIC improvements enhance practicality and sensitivity.
    • Assays now possess improved quantitative attributes.
    • Detection of prion seeding activity in dilute, inhibitor-laden fluids like blood plasma is promoted.

    Conclusions:

    • RT-QuIC-based assays are powerful tools for prion disease diagnosis.
    • Assay enhancements expand their utility to complex biological samples.
    • Further development promises more accessible and sensitive prion detection methods.