Gerstmann-Straussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments.

ABSTRACT: Despite their phenotypic heterogeneity, most human prion diseases belong to two broadly defined groups: Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker disease (GSS). While the structural characteristics of the disease-related proteinase K-resistant prion protein (resPrP^D) associated with the CJD group are fairly well established, many features of GSS-associated resPrP^D are unclear. Electrophoretic profiles of resPrP^D associated with GSS variants typically show 6-8 kDa bands corresponding to the internal PrP fragments as well as a variable number of higher molecular weight bands, the molecular nature of which has not been investigated. Here we have performed systematic studies of purified resPrP^D species extracted from GSS case

SUBMITTER: Cracco L 

PROVIDER: S-EPMC6540574 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature