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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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Materias: | |
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 |
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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