A sensitive filter retention assay for the detection of PrPSc and the screening of anti‐prion compounds
- 10 August 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 503 (1), 41-45
- https://doi.org/10.1016/s0014-5793(01)02692-8
Abstract
A hallmark of prion diseases is the accumulation of an abnormally folded prion protein, denoted PrP Sc . Here we describe a new and highly sensitive method for the detection of PrP Sc in brain and other tissue samples that utilizes both PrP Sc diagnostic criteria in combination; protease resistance and aggregation. Upon filtration of tissue extracts derived from scrapie- or bovine spongiform encephalopathy-infected animals, PrP Sc is retained and detected on the membranes. Laborious steps such as SDS–PAGE and Western blotting are avoided with concomitant gain in sensitivity and reliability. The new procedure also proved useful in a screen for anti-prion compounds in a scrapie-infected cell culture model.Keywords
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