Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2013-02-01
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| Series: | Pathogens |
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| Online Access: | http://www.mdpi.com/2076-0817/2/1/92 |
| _version_ | 1811277958894059520 |
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| author | Takashi Yokoyama Shirou Mohri Morikazu Imamura Yoshifumi Iwamaru Kentaro Masujin Kazuo Kasai |
| author_facet | Takashi Yokoyama Shirou Mohri Morikazu Imamura Yoshifumi Iwamaru Kentaro Masujin Kazuo Kasai |
| author_sort | Takashi Yokoyama |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T00:26:09Z |
| format | Article |
| id | doaj.art-db744cc4e18f4275b78ecd5480d34a13 |
| institution | Directory Open Access Journal |
| issn | 2076-0817 |
| language | English |
| last_indexed | 2024-04-13T00:26:09Z |
| publishDate | 2013-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pathogens |
| spelling | doaj.art-db744cc4e18f4275b78ecd5480d34a132022-12-22T03:10:37ZengMDPI AGPathogens2076-08172013-02-01219210410.3390/pathogens2010092Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie StrainTakashi YokoyamaShirou MohriMorikazu ImamuraYoshifumi IwamaruKentaro MasujinKazuo KasaiThe 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.http://www.mdpi.com/2076-0817/2/1/92prionChandlersmall PrPSc aggregateconformational stabilityPK sensitivity |
| spellingShingle | Takashi Yokoyama Shirou Mohri Morikazu Imamura Yoshifumi Iwamaru Kentaro Masujin Kazuo Kasai Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain Pathogens prion Chandler small PrPSc aggregate conformational stability PK sensitivity |
| title | Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain |
| title_full | Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain |
| title_fullStr | Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain |
| title_full_unstemmed | Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain |
| title_short | Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain |
| title_sort | heterogeneity of the abnormal prion protein prpsc of the chandler scrapie strain |
| topic | prion Chandler small PrPSc aggregate conformational stability PK sensitivity |
| url | http://www.mdpi.com/2076-0817/2/1/92 |
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