Bioassays and Inactivation of Prions
Bioassays and Inactivation of Prions
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DOI：
10.1101/cshperspect.a023499
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发表时间：
2017-08-01
影响因子：
7.2
通讯作者：
Prusiner, Stanley B.
中科院分区：
文献类型：
--
作者：
Giles, Kurt;Woerman, Amanda L.;Prusiner, Stanley B.
朊病毒的实验研究需要一个模型来描述它们的传播。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，耗时的动物生物测定是测量感染性的唯一选择。虽然已经开发了细胞模型和其他体外工具来繁殖朊病毒，但它们都有局限性，动物生物测定仍然是测量感染性的金标准。最近的大量数据认为，β-淀粉样蛋白（A β）和tau蛋白都形成了导致阿尔茨海默病的朊病毒，α-突触核蛋白形成了导致多系统萎缩和帕金森病的朊病毒。细胞和动物模型重现了细胞间传播的一些关键特征，现在可以测量不同的朊病毒株。
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 beta-amyloid (A beta) and tau proteins form prions that cause Alzheimer's disease, and alpha-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.