Gerstmann-sträussler-scheinker disease and anchorless prion protein mice share prion conformational properties diverging from sporadic creutzfeldt-jakob disease

Abstract

Background: Prion strains exhibit distinct physical and biochemical repertoires, aggregation propensity, and biological properties. Results: A biochemical approach is developed for defining the conformational features of prions with or without glycosylphosphatidylinositol (GPI)-anchor. Conclusion: GPI anchorless prions are detected in human genetic prion diseases, but not in sporadic forms. Significance: Unveiling the structure of GPI anchorless prions to predict pathological properties. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.