title: Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain.
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.
authors.affiliation: Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. kakasai@affrc.go.jp.
authors.forename: Kazuo
authors.initials: K
authors.lastname: Kasai
authors.affiliation: Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. gan@affrc.go.jp.
authors.forename: Yoshifumi
authors.initials: Y
authors.lastname: Iwamaru
authors.affiliation: Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. masujin@affrc.go.jp.
authors.forename: Kentaro
authors.initials: K
authors.lastname: Masujin
authors.affiliation: Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. imamuram@affrc.go.jp.
authors.forename: Morikazu
authors.initials: M
authors.lastname: Imamura
authors.affiliation: Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. shirou@affrc.go.jp.
authors.forename: Shirou
authors.initials: S
authors.lastname: Mohri
authors.affiliation: Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. tyoko@affrc.go.jp.
authors.forename: Takashi
authors.initials: T
authors.lastname: Yokoyama