Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain

被引：1

作者：

Kasai, Kazuo ^{[1
]}

Iwamaru, Yoshifumi ^{[1
]}

Masujin, Kentaro ^{[1
]}

Imamura, Morikazu ^{[1
]}

Mohri, Shirou ^{[1
]}

Yokoyama, Takashi ^{[1
]}

机构：

[1] Natl Inst Anim Hlth, Prion Dis Res Ctr, Tsukuba, Ibaraki 3050856, Japan

来源：

PATHOGENS | 2013年 / 2卷 / 01期

关键词：

prion; Chandler; small PrPSc aggregate; conformational stability; PK sensitivity;

D O I：

10.3390/pathogens2010092

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：92 / +

页数：13

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