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A sensitive filter retention assay for the detection of PrP Sc and the screening of anti‐prion compounds
Author(s) -
Winklhofer Konstanze F,
Hartl F.Ulrich,
Tatzelt Jörg
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02692-8
Subject(s) - chemistry , chromatography , microbiology and biotechnology , biology
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.