Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) 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, previ...

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Detalles Bibliográficos
Autores principales: Kasai, Kazuo, Iwamaru, Yoshifumi, Masujin, Kentaro, Imamura, Morikazu, Mohri, Shirou, Yokoyama, Takashi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4235706/
https://www.ncbi.nlm.nih.gov/pubmed/25436883
http://dx.doi.org/10.3390/pathogens2010092
Descripción
Sumario: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).

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