2013年2月
Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science
JOURNAL OF BIOCHEMISTRY
- ,
- ,
- 巻
- 153
- 号
- 2
- 開始ページ
- 139
- 終了ページ
- 145
- 記述言語
- 英語
- 掲載種別
- 書評論文,書評,文献紹介等
- DOI
- 10.1093/jb/mvs148
- 出版者・発行元
- OXFORD UNIV PRESS
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are fatal infectious neurodegenerative disorders. Their causative agents are prions, which are composed of disease-associated forms of prion protein (PrPSc). Naturally occurring cases of TSEs are found in several mammalian species including humans, sheep, goats, minks, cattle and deer. Prions are also experimentally transmissible to other mammals such as mice, hamsters and monkeys, but interspecies transmission is often inefficient due to the 'species-barrier'. Studies have suggested that the barrier is not only simply determined by differences in amino acid sequences of cellular PrP (PrPC) among animal species, but also by prion strains which are closely associated with conformational properties of PrPSc aggregates. Although the conformational properties of PrPSc remain largely unknown, recent investigation of local structures of PrPC and, in particular, structural modelling of PrPSc aggregates have provided molecular insight into this field. In this review, we discuss the species-barrier phenomenon in terms of the protein science.
- リンク情報
- ID情報
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- DOI : 10.1093/jb/mvs148
- ISSN : 0021-924X
- Web of Science ID : WOS:000314119500002