Next Article in Journal
Microbiological Values of Rainwater Harvested in Adelaide
Next Article in Special Issue
Pharmacological Agents Targeting the Cellular Prion Protein
Previous Article in Journal
Pathogenesis and Animal Models of Post-Primary (Bronchogenic) Tuberculosis, A Review
Previous Article in Special Issue
Prion Strains and Transmission Barrier Phenomena
Article Menu

Export Article

Open AccessFeature PaperReview
Pathogens 2018, 7(1), 20; https://doi.org/10.3390/pathogens7010020

The Structure of PrPSc Prions

1
Centre for Prions and Protein Folding Diseases & Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2M8, Canada
2
CIMUS Biomedical Research Institute & Department of Medical Sciences, University of Santiago de Compostela-IDIS, 15782 Santiago de Compostela, Spain
*
Author to whom correspondence should be addressed.
Received: 22 January 2018 / Revised: 31 January 2018 / Accepted: 3 February 2018 / Published: 7 February 2018
(This article belongs to the Special Issue PrPSc prions: state of the art)
Full-Text   |   PDF [3347 KB, uploaded 7 February 2018]   |  

Abstract

PrPSc (scrapie isoform of the prion protein) prions are the infectious agent behind diseases such as Creutzfeldt–Jakob disease in humans, bovine spongiform encephalopathy in cattle, chronic wasting disease in cervids (deer, elk, moose, and reindeer), as well as goat and sheep scrapie. PrPSc is an alternatively folded variant of the cellular prion protein, PrPC, which is a regular, GPI-anchored protein that is present on the cell surface of neurons and other cell types. While the structure of PrPC is well studied, the structure of PrPSc resisted high-resolution determination due to its general insolubility and propensity to aggregate. Cryo-electron microscopy, X-ray fiber diffraction, and a variety of other approaches defined the structure of PrPSc as a four-rung β-solenoid. A high-resolution structure of PrPSc still remains to be solved, but the four-rung β-solenoid architecture provides a molecular framework for the autocatalytic propagation mechanism that gives rise to the alternative conformation of PrPSc. Here, we summarize the current knowledge regarding the structure of PrPSc and speculate about the molecular conversion mechanisms that leads from PrPC to PrPSc. View Full-Text
Keywords: PrPSc; prion structure; β-solenoid; cryo-electron microscopy; prion propagation; amyloid PrPSc; prion structure; β-solenoid; cryo-electron microscopy; prion propagation; amyloid
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Wille, H.; Requena, J.R. The Structure of PrPSc Prions. Pathogens 2018, 7, 20.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Pathogens EISSN 2076-0817 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top