ABSTRACT
The conversion of a normal membrane glycoprotein, the cellular prion protein (PrPC), to an insoluble aggregated isoform (PrPSc) is thought to be the key process in the pathogenesis of transmissible spongiform encephalopathies (TSEs) (1). Consequently, the specific detection of PrPSc has formed the basis for the biochemical diagnosis of TSEs, which include bovine spongiform encephalopathy (BSE), scrapie in sheep, and Creutzfeld-Jacob disease (CJD) in humans (2).
