1887

Abstract

Infectivity associated with prion disease has been demonstrated in blood throughout the course of disease, yet the ability to detect blood-borne prions by methods remains challenging. We capitalized on longitudinal pathogenesis studies of chronic wasting disease (CWD) conducted in the native host to examine haematogenous prion load by real-time quaking-induced conversion (RT-QuIC) and protein misfolding cyclic amplification. Our study demonstrated detection of amyloid seeding activity (prions) in buffy-coat cells harvested from deer orally dosed with low concentrations of CWD positive (+) brain (1 gr and 300 ng) or saliva (300 ng RT-QuIC equivalent). These findings make possible the longitudinal assessment of prion disease and deeper investigation of the role haematogenous prions play in prion pathogenesis.

Funding
This study was supported by the:
  • National Institutes of Health (Award R01-AI-112956)
    • Principle Award Recipient: Not Applicable
  • National Institutes of Health (Award R01-NS-061902)
    • Principle Award Recipient: Not Applicable
  • National Institutes of Health (Award R01-AI-093634)
    • Principle Award Recipient: Not Applicable
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2019-12-17
2024-04-25
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