Morales Rodrigo, Callegari Keri, Soto Claudio
Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, 6431 Fannin Street, Houston, TX 77030, United States.
Virus Res. 2015 Sep 2;207:106-12. doi: 10.1016/j.virusres.2014.12.031. Epub 2015 Jan 6.
Recent findings have shown that several misfolded proteins can transmit disease pathogenesis in a prion-like manner by transferring their conformational properties to normally folded units. However, the extent by which these molecule-to-molecule or cell-to-cell spreading processes reflect the entire prion behavior is now subject of controversy, especially due to the lack of epidemiological data supporting inter-individual transmission of non-prion protein misfolding diseases. Nevertheless, extensive research has shown that several of the typical characteristics of prions can be observed for Aβ and tau aggregates when administered in animal models. In this article we review recent studies describing the prion-like features of both proteins, highlighting the similarities with bona fide prions in terms of inter-individual transmission, their strain-like conformational diversity, and the transmission of misfolded aggregates by different routes of administration.
最近的研究结果表明，几种错误折叠的蛋白质可以通过将其构象特性传递给正常折叠的单元，以朊病毒样的方式传播疾病发病机制。然而，这些分子间或细胞间传播过程在多大程度上反映了整个朊病毒行为，目前仍存在争议，特别是由于缺乏支持非朊病毒蛋白错误折叠疾病个体间传播的流行病学数据。尽管如此，广泛的研究表明，当在动物模型中施用时，Aβ和tau聚集体可以观察到朊病毒的几个典型特征。在本文中，我们回顾了最近描述这两种蛋白质朊病毒样特征的研究，强调了在个体间传播、菌株样构象多样性以及通过不同给药途径传播错误折叠聚集体方面与真正朊病毒的相似性。
