Next Article in Journal
Zika Virus Trafficking and Interactions in the Human Male Reproductive Tract
Previous Article in Journal
Molecular Responses to the Zika Virus in Mosquitoes
Previous Article in Special Issue
Pharmacological Agents Targeting the Cellular Prion Protein
Open AccessFeature PaperEditor’s ChoiceReview

Comparing the Folds of Prions and Other Pathogenic Amyloids

Department of Biochemistry & Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, AB T6G 2M8, Canada
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Pathogens 2018, 7(2), 50; https://doi.org/10.3390/pathogens7020050
Received: 16 April 2018 / Revised: 29 April 2018 / Accepted: 2 May 2018 / Published: 4 May 2018
(This article belongs to the Special Issue PrPSc prions: state of the art)
Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-β(1-42) (Aβ(1-42)) fibrils, and α-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrPSc as a 4-rung β-solenoid. Thus, the structure of PrPSc must have a high similarity to that of the fungal prion HET-s, which is part of the fungal heterokaryon incompatibility system and contains a 2-rung β-solenoid. This review compares the structures of tau PHFs, Aβ(1-42), and α-synuclein fibrils, where the β-strands of each molecule stack on top of each other in a parallel in-register arrangement, with the β-solenoid folds of HET-s and PrPSc. View Full-Text
Keywords: prion structure; β-solenoid; PHF-tau structure; Aβ(1-42) fibril structure; α-synuclein amyloid structure; parallel in-register β-structure prion structure; β-solenoid; PHF-tau structure; Aβ(1-42) fibril structure; α-synuclein amyloid structure; parallel in-register β-structure
Show Figures

Figure 1

MDPI and ACS Style

Flores-Fernández, J.M.; Rathod, V.; Wille, H. Comparing the Folds of Prions and Other Pathogenic Amyloids. Pathogens 2018, 7, 50.

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.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop