Acc Chem Res. 2006 Sep;39(9):654-62.

The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro.

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Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106, USA. witold.surewicz@case.edu

Erratum in

Acc Chem Res. 2006 Nov;39(11):879-80.

Abstract

Self-perpetuating conformational conversion of the cellular prion protein PrP(C) into the beta-sheet-rich "scrapie" conformer (PrP(Sc)) is believed to be the central molecular event in pathogenesis of a group of diseases known as transmissible spongiform encephalopathies. Recent advances provide growing support for the notion that a misfolded protein alone might act as an infectious agent. Furthermore, findings regarding the mechanism of prion protein structural rearrangement, the role of folding intermediates in conformational conversion, and "conformational adaptability" in the propagation of prion amyloids in vitro yield molecular-level insight into such phenomena as inherited prion diseases, prion transmission barriers, and prion strains.

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