Ludwig-Maximilians-Universität, Chair of Metabolic Biochemistry

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A sensitive filter retention assay for the detection of PrP(Sc) and the screening of anti-prion compounds

FEBS Lett 503(1): 41-5

Authors/Editors: Winklhofer KF
Hartl FU
Publication Date: 2001
Type of Publication: Journal Article
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.

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