Ryou Chongsuk, Mays Charles E
Sanders Brown Center on Aging and Department of Microbiology, Immunology & Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY 40536, USA.
Int J Med Sci. 2008;5(6):347-53. doi: 10.7150/ijms.5.347. Epub 2008 Nov 11.
Prion diseases are caused by proteinaceous pathogens termed prions. Although the details of the mechanism of prion propagation are not fully understood, conformational conversion of cellular prion protein (PrP(C)) to misfolded, disease-associated scrapie prion protein (PrP(Sc)) is considered the essential biochemical event for prion replication. Currently, studying prion replication in vitro is difficult due to the lack of a system which fully recapitulates the in vivo phenomenon. Over the last 15 years, a number of in vitro systems supporting PrP(C) conversion, PrP(Sc) amplification, or amyloid fibril formation have been established. In this review, we describe the evolving methodology of in vitro prion propagation assays and discuss their ability in reflecting prion propagation in vivo.
朊病毒疾病由被称为朊病毒的蛋白质病原体引起。尽管朊病毒传播机制的细节尚未完全明了,但细胞朊蛋白(PrP(C))向错误折叠的、与疾病相关的瘙痒病朊病毒蛋白(PrP(Sc))的构象转变被认为是朊病毒复制的关键生化事件。目前,由于缺乏能完全重现体内现象的系统,体外研究朊病毒复制很困难。在过去15年里,已建立了许多支持PrP(C)转化、PrP(Sc)扩增或淀粉样纤维形成的体外系统。在这篇综述中,我们描述了体外朊病毒传播测定方法的演变,并讨论了它们反映体内朊病毒传播的能力。