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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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
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author Kasai, Kazuo
Iwamaru, Yoshifumi
Masujin, Kentaro
Imamura, Morikazu
Mohri, Shirou
Yokoyama, Takashi
author_facet Kasai, Kazuo
Iwamaru, Yoshifumi
Masujin, Kentaro
Imamura, Morikazu
Mohri, Shirou
Yokoyama, Takashi
author_sort Kasai, Kazuo
collection PubMed
description 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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spelling pubmed-42357062014-11-25 Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain Kasai, Kazuo Iwamaru, Yoshifumi Masujin, Kentaro Imamura, Morikazu Mohri, Shirou Yokoyama, Takashi Pathogens Article 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). MDPI 2013-02-18 /pmc/articles/PMC4235706/ /pubmed/25436883 http://dx.doi.org/10.3390/pathogens2010092 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Kasai, Kazuo
Iwamaru, Yoshifumi
Masujin, Kentaro
Imamura, Morikazu
Mohri, Shirou
Yokoyama, Takashi
Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain
title Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain
title_full Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain
title_fullStr Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain
title_full_unstemmed Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain
title_short Heterogeneity of the Abnormal Prion Protein (PrP(Sc)) of the Chandler Scrapie Strain
title_sort heterogeneity of the abnormal prion protein (prp(sc)) of the chandler scrapie strain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4235706/
https://www.ncbi.nlm.nih.gov/pubmed/25436883
http://dx.doi.org/10.3390/pathogens2010092
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