Bacteriophage-encoded chaperonins stimulate prion protein fibrillation in an ATP-dependent manner

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS
Evgeniia V. Leisi , Andrey V. Moiseenko , Sofia S. Kudryavtseva , Denis V. Pozdyshev , Vladimir I. Muronetz , Lidia P. Kurochkina
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引用次数: 1

Abstract

The pathogenesis of the various prion diseases is based on the conformational conversion of the prion protein from its physiological cellular form to the insoluble scrapie isoform. Several chaperones, including the Hsp60 family of group I chaperonins, are known to contribute to this transformation, but data on their effects are scarce and conflicting. In this work, two GroEL-like phage chaperonins, the single-ring OBP and the double-ring EL, were found to stimulate monomeric prion protein fibrillation in an ATP-dependent manner. The resulting fibrils were characterised by thioflavin T fluorescence, electron microscopy, proteinase K digestion assay and other methods. In the presence of ATP, chaperonins were found to promote the conversion of prion protein monomers into short amyloid fibrils with their further aggregation into less toxic large clusters. Fibrils generated with the assistance of phage chaperonins differ in morphology and properties from those formed spontaneously from monomeric prion in the presence of denaturants at acidic pH.

Abstract Image

噬菌体编码的伴侣蛋白以ATP依赖的方式刺激朊病毒蛋白纤颤。
各种朊病毒疾病的发病机制是基于朊病毒蛋白从其生理细胞形式向不溶性瘙痒异构体的构象转换。已知几种伴侣蛋白,包括I组伴侣蛋白的Hsp60家族,对这种转化有贡献,但关于其影响的数据很少且相互矛盾。在这项工作中,发现两种GroEL样噬菌体伴侣蛋白,单环OBP和双环EL,以ATP依赖的方式刺激单体朊病毒蛋白纤颤。通过硫黄素T荧光、电子显微镜、蛋白酶K消化测定和其他方法对所得原纤维进行了表征。在ATP存在的情况下,发现伴侣蛋白促进朊病毒蛋白单体转化为短淀粉样原纤维,并进一步聚集成毒性较小的大簇。在噬菌体伴侣蛋白的帮助下产生的纤维蛋白在形态和性质上与在酸性pH下变性剂存在下由单体朊病毒自发形成的纤维蛋白不同。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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