The pathological prion protein, PrPSc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrPSc aggregates of mouse-adapted prion strains. We showed that small PrPSc aggregates, previously thought to be PK-sensitive, are resistant to PK digestion. Furthermore, we showed that small PrPSc aggregates of the Chandler scrapie strain have greater resistance to PK digestion and aggregation-denaturation than large PrPSc aggregates of this strain. We conclude that this strain consists of heterogeneous PrPSc.
Kasai, K., Iwamaru, Y., Masujin, K., Imamura, M., Mohri, S., & Yokoyama, T. (2013). Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain. Pathogens, 2(1), 92–104. https://doi.org/10.3390/pathogens2010092