Harris David A, True Heather L
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Neuron. 2006 May 4;50(3):353-7. doi: 10.1016/j.neuron.2006.04.020.
Prion diseases in humans and animals are due to conformational conversion of PrP(C), a cellular glycoprotein of unknown function, into PrP(Sc), an isoform that appears to be infectious in the absence of nucleic acids. Proteins that behave as prions are also found in yeast and filamentous fungi. Although there is now strong experimental support for the hypothesis that prions are infectious proteins, two subjects have remained poorly understood: the structure of prions, and the mechanisms by which they kill neurons. In this review, we will highlight recent studies that shed new light on these important issues.
人和动物的朊病毒疾病是由于细胞糖蛋白PrP(C)（一种功能未知的细胞糖蛋白）构象转变为PrP(Sc)，PrP(Sc)是一种在没有核酸的情况下似乎具有传染性的异构体。在酵母和丝状真菌中也发现了表现为朊病毒的蛋白质。尽管现在有强有力的实验支持朊病毒是传染性蛋白质这一假说，但仍有两个问题了解甚少：朊病毒的结构以及它们杀死神经元的机制。在这篇综述中，我们将重点介绍最近对这些重要问题有新见解的研究。
