Galkin A P, Velizhanina M E, Sopova Yu V, Shenfeld A A, Zadorsky S P
St. Petersburg Branch of Vavilov Institute of General Genetics, Russian Academy of Sciences, St. Petersburg, 199034, Russia.
St. Petersburg State University, Department of Genetics and Biotechnology, St. Petersburg, 199034, Russia.
Biochemistry (Mosc). 2018 Oct;83(10):1184-1195. doi: 10.1134/S0006297918100048.
Amyloids are highly ordered aggregates of protein fibrils exhibiting cross-β structure formed by intermolecular hydrogen bonds. Pathological amyloid deposition is associated with the development of several socially significant incurable human diseases. Of particular interest are infectious amyloids, or prions, that cause several lethal neurodegenerative diseases in humans and can be transmitted from one organism to another. Because of almost complete absence of criteria for infectious and non-infectious amyloids, there is a lack of consensus, especially, in the definition of similarities and differences between prions and non-infectious amyloids. In this review, we formulated contemporary molecular-biological criteria for identification of prions and non-infectious amyloids and focused on explaining the differences between these two types of molecules.
淀粉样蛋白是由分子间氢键形成的具有交叉β结构的高度有序的蛋白质原纤维聚集体。病理性淀粉样蛋白沉积与几种具有社会意义的人类不治之症的发展有关。特别令人感兴趣的是传染性淀粉样蛋白,即朊病毒,它会导致人类多种致命的神经退行性疾病,并且可以从一个生物体传播到另一个生物体。由于几乎完全缺乏区分传染性和非传染性淀粉样蛋白的标准,因此缺乏共识,尤其是在朊病毒和非传染性淀粉样蛋白之间异同的定义方面。在本综述中,我们制定了用于鉴定朊病毒和非传染性淀粉样蛋白的当代分子生物学标准,并着重解释这两种分子之间的差异。