Department of Computing Science, University of Alberta, Edmonton, Alberta, Canada; Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada; National Institute for Nanotechnology, Edmonton, Alberta, Canada.
Department of Computing Science, University of Alberta, Edmonton, Alberta, Canada; National Institute for Nanotechnology, Edmonton, Alberta, Canada.
PLoS One. 2014 Jun 3;9(6):e98753. doi: 10.1371/journal.pone.0098753. eCollection 2014.
The formation of β-sheet rich prion oligomers and fibrils from native prion protein (PrP) is thought to be a key step in the development of prion diseases. Many methods are available to convert recombinant prion protein into β-sheet rich fibrils using various chemical denaturants (urea, SDS, GdnHCl), high temperature, phospholipids, or mildly acidic conditions (pH 4). Many of these methods also require shaking or another form of agitation to complete the conversion process. We have identified that shaking alone causes the conversion of recombinant PrP to β-sheet rich oligomers and fibrils at near physiological pH (pH 5.5 to pH 6.2) and temperature. This conversion does not require any denaturant, detergent, or any other chemical cofactor. Interestingly, this conversion does not occur when the water-air interface is eliminated in the shaken sample. We have analyzed shaking-induced conversion using circular dichroism, resolution enhanced native acidic gel electrophoresis (RENAGE), electron microscopy, Fourier transform infrared spectroscopy, thioflavin T fluorescence and proteinase K resistance. Our results show that shaking causes the formation of β-sheet rich oligomers with a population distribution ranging from octamers to dodecamers and that further shaking causes a transition to β-sheet fibrils. In addition, we show that shaking-induced conversion occurs for a wide range of full-length and truncated constructs of mouse, hamster and cervid prion proteins. We propose that this method of conversion provides a robust, reproducible and easily accessible model for scrapie-like amyloid formation, allowing the generation of milligram quantities of physiologically stable β-sheet rich oligomers and fibrils. These results may also have interesting implications regarding our understanding of prion conversion and propagation both within the brain and via techniques such as protein misfolding cyclic amplification (PMCA) and quaking induced conversion (QuIC).
β-折叠丰富的朊病毒寡聚物和纤维的形成被认为是朊病毒病发展的关键步骤。有许多方法可将重组朊病毒蛋白转化为富含β-折叠的纤维,使用各种化学变性剂(尿素、SDS、GdnHCl)、高温、磷脂或微酸性条件(pH4)。许多这些方法还需要摇晃或其他形式的搅拌来完成转化过程。我们已经确定,仅摇晃就可以在接近生理 pH(pH5.5 至 pH6.2)和温度下将重组 PrP 转化为富含β-折叠的寡聚物和纤维。这种转化不需要任何变性剂、洗涤剂或任何其他化学辅助因子。有趣的是,当在摇晃的样品中消除水-气界面时,这种转化不会发生。我们使用圆二色性、分辨率增强的天然酸性凝胶电泳(RENAGE)、电子显微镜、傅里叶变换红外光谱、硫黄素 T 荧光和蛋白酶 K 抗性分析了摇晃诱导的转化。我们的结果表明,摇晃会导致富含β-折叠的寡聚物的形成,其种群分布范围从八聚体到十二聚体,进一步摇晃会导致向β-折叠纤维的转变。此外,我们表明,摇晃诱导的转化发生在广泛的全长和截断的鼠、仓鼠和鹿朊病毒蛋白的构建体中。我们提出,这种转化方法为类瘙痒样淀粉样形成提供了一种强大、可重复且易于获得的模型,允许生成毫克量的生理稳定的富含β-折叠的寡聚物和纤维。这些结果可能对我们理解朊病毒的转化和传播,无论是在大脑内还是通过蛋白质错误折叠循环扩增(PMCA)和震颤诱导转化(QuIC)等技术,都具有有趣的意义。