A sensitive filter retention assay for the detection of PrPSc and the screening of anti-prion compounds

A hallmark of prion diseases is the accumulation of an abnormally folded pr ion protein, denoted PrPSc. Here we describe a new and highly sensitive met hod for the detection of PrPSc in brain and other tissue samples that utili zes both PrPSc diagnostic criteria in combination; protease resistance and aggregation. Upon filtration of tissue extracts derived from scrapie- or bo vine spongiform encephalopathy-infected animals, PrPSc is retained and dete cted on the membranes. Laborious steps such as SDS-PAGE and Western blottin g are avoided with concomitant gain in sensitivity and reliability. The new procedure also proved useful in a screen for anti-prion compounds in a scr apie-infected cell culture model. (C) 2001 Published by Elsevier Science B. V. on behalf of the Federation of European Biochemical Societies.