Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain

The pathological prion protein, PrP Sc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrP Sc aggregates of mouse-adapted prion strains. We showed that small PrP Sc aggregates, previously thought to be PK-sensitive, are resistant to PK digestion. Furthermore, we showed that small PrP Sc aggregates of the Chandler scrapie strain have greater resistance to PK digestion and aggregation-denaturation than large PrP Sc aggregates of this strain. We conclude that this strain consists of heterogeneous PrP Sc.