Published January 23, 2024 | Version v1
Dataset Open

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

Creators

  • 1. ROR icon CIC bioGUNE
  • 2. Atlas Molecular Pharma (Spain)
  • 3. Centro de Investigación Biomédica en Red de Enfermedades infecciosas (CIBERINFEC)
  • 4. ATLAS Molecular Pharma (Spain)
  • 5. ROR icon Institute for Research and Technology in Food and Agriculture
  • 6. ROR icon Centre de Recerca en Sanitat Animal
  • 7. Hospital Universitario Araba sede Txagorritxu
  • 8. Hospital Universitario Cruces
  • 9. ROR icon Colorado State University
  • 10. ROR icon NEIKER, the Basque Institute for Agricultural Research and Development
  • 11. ROR icon Ikerbasque

Description

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.

Files

Figure 3.zip

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