一种评估氨基酸序列对朊病毒蛋白错误折叠倾向影响的快速方法。

A Quick Method to Evaluate the Effect of the Amino Acid Sequence in the Misfolding Proneness of the Prion Protein.

作者信息

Fernández-Borges Natalia, Eraña Hasier, Elezgarai Saioa R, Harrathi Chafik, Venegas Vanesa, Castilla Joaquín

机构信息

CIC bioGUNE, Parque Tecnológico de Bizkaia, Derio, 48160, Bizkaia, Spain.

IKERBASQUE, Basque Foundation for Science, Bilbao, 48013, Bizkaia, Spain.

出版信息

Methods Mol Biol. 2017;1658:205-216. doi: 10.1007/978-1-4939-7244-9_15.

DOI:10.1007/978-1-4939-7244-9_15

PMID:28861792

Abstract

Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative diseases where the misfolding of the prion protein (PrP) is a crucial event. Based on studies in TSE-affected humans and the generation of transgenic mouse models overexpressing different mutated versions of the PrP, we conclude that both wild-type and mutated PrPs exhibit differential propensity to misfold in vivo. Here, we describe a new method in vitro to assess and quantify the PrP misfolding phenomenon in order to better understand the molecular mechanisms involved in this process.

摘要

朊病毒病或传染性海绵状脑病（TSEs）是一组神经退行性疾病，其中朊病毒蛋白（PrP）的错误折叠是一个关键事件。基于对受TSE影响的人类的研究以及对过表达不同突变版本PrP的转基因小鼠模型的构建，我们得出结论，野生型和突变型PrP在体内均表现出不同的错误折叠倾向。在此，我们描述一种体外新方法，用于评估和量化PrP错误折叠现象，以便更好地理解该过程中涉及的分子机制。