ABSTRACT
The identification of (a) the pathological prion protein (PrPSc) in the brain of animals affected by scrapie, (b) the posterior localization of the gene, and (c) the normal version of the prion protein (PrPC) led to a great amount of work to understand the differences between the two PrP isoforms and the mechanism by which the normal protein is converted into the disease-associated protein. This chapter describes the current knowledge about the structural properties of PrP isoforms and the mechanism by which prions propagate in the body by transmission of protein misfolding.
