Source Data Files from publication: A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of infectious prions, Nature Communications 2024

This Dataset contains all the Source Data corresponding to the results from the manuscript entitled "A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of infectious prions", accepted for publication in Nature Communications Journal. The dataset includes uncropped scans of all gels and blots used to generated the final figures and tables (including Supplementary figures and tables), as well as the raw data used to generate the plots shown in the manuscript.

The dataset is organized by Figures and Tables, with the source data files containing all the information used in each figure or table included in a compressed (.zip) file. The figure and table numbering used in the manuscript is kept, with source data available for: Figures 1 & 2, Figure 3, Supplementary figure 1, Supplementary figure 2,  Supplementary figure 3, and Supplementary figure 4.

Manuscript abstract:

Prion diseases are a group of rapidly progressing neurodegenerative disorders caused by the misfolding of the endogenous prion protein (PrPC) into a pathogenic form (PrPSc). This process, despite being the central event underlying these disorders, remains largely unknown at a molecular level, precluding the prediction of new potential outbreaks or interspecies transmission incidents.

In this work, we present a method to generate infectious bona fide recombinant prions de novo, allowing a comprehensive analysis of protein misfolding across a wide range of prion proteins from mammalian species. We studied more than 380 different prion proteins from mammals and classified them according to their spontaneous misfolding propensity and their conformational variability.

This study aims to address fundamental questions in the prion research field such as defining infectivity determinants, interspecies transmission barriers or the structural influence of specific amino acids and provides invaluable information for future diagnosis and therapy applications.

本数据集包含与已被《自然·通讯》（Nature Communications）期刊录用的题为《基于蛋白质错误折叠震荡扩增技术自发产生数百种传染性朊病毒》的手稿结果对应的全部源数据。数据集涵盖用于生成最终图表与表格（含补充图表与表格）的所有凝胶与印迹膜未裁剪扫描件，以及手稿中各类绘图所用的原始数据。

本数据集按图表与表格进行分类组织，每个图表或表格对应的全部源信息均收纳于压缩（.zip）格式文件中。手稿沿用了原有的图表编号，可获取源数据的内容包括：图1与图2、图3、补充图1、补充图2、补充图3及补充图4。

手稿摘要：
朊病毒病是一类由内源性朊蛋白（prion protein, PrP^C）错误折叠为致病型朊蛋白（PrP^Sc）所引发的快速进展性神经退行性疾病。尽管该过程是此类疾病的核心发病事件，但其分子层面的具体机制仍未完全明晰，阻碍了对新型潜在暴发事件或跨物种传播事件的预测。

本研究提出一种可从头（de novo）生成具有感染性的天然重组朊病毒的方法，能够全面分析多种哺乳动物朊蛋白的蛋白质错误折叠过程。我们共研究了超过380种不同的哺乳动物朊蛋白，并根据其自发错误折叠倾向与构象变异性对其进行了分类。

本研究旨在解答朊病毒研究领域的若干基础科学问题，例如确定感染性决定簇、跨物种传播屏障，或是特定氨基酸的结构影响，并为未来的诊断与治疗应用提供极具价值的参考信息。