Giles Kurt, Woerman Amanda L, Berry David B, Prusiner Stanley B
Institute for Neurodegenerative Diseases, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, California 94158.
Department of Neurology, University of California, San Francisco, San Francisco, California 94158.
Cold Spring Harb Perspect Biol. 2017 Aug 1;9(8):a023499. doi: 10.1101/cshperspect.a023499.
The experimental study of prions requires a model for their propagation. However, because prions lack nucleic acids, the simple techniques used to replicate bacteria and viruses are not applicable. For much of the history of prion research, time-consuming bioassays in animals were the only option for measuring infectivity. Although cell models and other in vitro tools for the propagation of prions have been developed, they all suffer limitations, and animal bioassays remain the gold standard for measuring infectivity. A wealth of recent data argues that both β-amyloid (Aβ) and tau proteins form prions that cause Alzheimer's disease, and α-synuclein forms prions that cause multiple system atrophy and Parkinson's disease. Cell and animal models that recapitulate some of the key features of cell-to-cell spreading and distinct strains of prions can now be measured.
朊病毒的实验研究需要一个其传播的模型。然而，由于朊病毒缺乏核酸，用于复制细菌和病毒的简单技术并不适用。在朊病毒研究的大部分历史中，在动物身上进行耗时的生物测定是测量传染性的唯一选择。尽管已经开发出用于朊病毒传播的细胞模型和其他体外工具，但它们都存在局限性，动物生物测定仍然是测量传染性的金标准。最近大量数据表明，β-淀粉样蛋白（Aβ）和tau蛋白都能形成导致阿尔茨海默病的朊病毒，而α-突触核蛋白能形成导致多系统萎缩和帕金森病的朊病毒。现在可以测量能够概括细胞间传播和不同朊病毒株一些关键特征的细胞和动物模型。
