Abstract: 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.
Keywords: prion; Chandler; small PrPSc aggregate; conformational stability; PK sensitivity
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Kasai, K.; Iwamaru, Y.; Masujin, K.; Imamura, M.; Mohri, S.; Yokoyama, T. Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain. Pathogens 2013, 2, 92-104.
Kasai K, Iwamaru Y, Masujin K, Imamura M, Mohri S, Yokoyama T. Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain. Pathogens. 2013; 2(1):92-104.
Kasai, Kazuo; Iwamaru, Yoshifumi; Masujin, Kentaro; Imamura, Morikazu; Mohri, Shirou; Yokoyama, Takashi. 2013. "Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain." Pathogens 2, no. 1: 92-104.