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Pathogens 2013, 2(1), 92-104; doi:10.3390/pathogens2010092

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

Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan
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Received: 9 January 2013 / Revised: 7 February 2013 / Accepted: 9 February 2013 / Published: 18 February 2013
(This article belongs to the Special Issue Prions)

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 prion; Chandler; small PrPSc aggregate; conformational stability; PK sensitivity
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

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.

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