Prions

被引:390
作者
Colby, David W. [1 ]
Prusiner, Stanley B. [1 ,2 ]
机构
[1] Univ Calif San Francisco, Inst Neurodegenerat Dis, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Dept Neurol, San Francisco, CA 94143 USA
来源
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY | 2011年 / 3卷 / 01期
关键词
CREUTZFELDT-JAKOB-DISEASE; CHRONIC WASTING DISEASE; FATAL FAMILIAL INSOMNIA; GERSTMANN-STRAUSSLER SYNDROME; BOVINE SPONGIFORM ENCEPHALOPATHY; INFECTED NEUROBLASTOMA-CELLS; CEREBELLAR PURKINJE-CELLS; SCRAPIE-ASSOCIATED FORM; AMYLOID PRECURSOR GENE; CENTRAL-NERVOUS-SYSTEM;
D O I
10.1101/cshperspect.a006833
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The discovery of infectious proteins, denoted prions, was unexpected. After much debate over the chemical basis of heredity, resolution of this issue began with the discovery that DNA, not protein, from pneumococcus was capable of genetically transforming bacteria (Avery et al. 1944). Four decades later, the discovery that a protein could mimic viral and bacterial pathogens with respect to the transmission of some nervous system diseases (Prusiner 1982) met with great resistance. Overwhelming evidence now shows that Creutzfeldt-Jakob disease (CJD) and related disorders are caused by prions. The prion diseases are characterized by neurodegeneration and lethality. In mammals, prions reproduce by recruiting the normal, cellular isoform of the prion protein (PrPC) and stimulating its conversion into the disease-causing isoform (PrPSc). PrPC and PrPSc have distinct conformations: PrPC is rich in alpha-helical content and has little beta-sheet structure, whereas PrPSc has less alpha-helical content and is rich in beta-sheet structure (Pan et al. 1993). The conformational conversion of PrPC to PrPSc is the fundamental event underlying prion diseases. In this article, we provide an introduction to prions and the diseases they cause.
引用
收藏
页码:1 / 22
页数:22
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