Next Article in Journal
Parvovirus B19 Uncoating Occurs in the Cytoplasm without Capsid Disassembly and It Is Facilitated by Depletion of Capsid-Associated Divalent Cations
Previous Article in Journal
NF-κB-Dependent Production of ROS and Restriction of HSV-1 Infection in U937 Monocytic Cells
Previous Article in Special Issue
Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast
Article Menu

Export Article

Open AccessReview

Heterogeneity and Architecture of Pathological Prion Protein Assemblies: Time to Revisit the Molecular Basis of the Prion Replication Process?

1
Molecular Virology and Immunology Unit (VIM), INRA, Université Paris-Saclay, 78350 Jouy-en-Josas, France
2
Laboratory of Physical Chemistry (LCP), UMR 8000 CNRS, Université Paris Sud, 91400 Orsay, France
*
Authors to whom correspondence should be addressed.
Viruses 2019, 11(5), 429; https://doi.org/10.3390/v11050429
Received: 17 April 2019 / Revised: 7 May 2019 / Accepted: 8 May 2019 / Published: 10 May 2019
(This article belongs to the Special Issue Deciphering the Molecular Targets of Prion and Prion-Like Strains)
  |  
PDF [1981 KB, uploaded 10 May 2019]
  |  

Abstract

Prions are proteinaceous infectious agents responsible for a range of neurodegenerative diseases in animals and humans. Prion particles are assemblies formed from a misfolded, β-sheet rich, aggregation-prone isoform (PrPSc) of the host-encoded cellular prion protein (PrPC). Prions replicate by recruiting and converting PrPC into PrPSc, by an autocatalytic process. PrPSc is a pleiomorphic protein as different conformations can dictate different disease phenotypes in the same host species. This is the basis of the strain phenomenon in prion diseases. Recent experimental evidence suggests further structural heterogeneity in PrPSc assemblies within specific prion populations and strains. Still, this diversity is rather seen as a size continuum of assemblies with the same core structure, while analysis of the available experimental data points to the existence of structurally distinct arrangements. The atomic structure of PrPSc has not been elucidated so far, making the prion replication process difficult to understand. All currently available models suggest that PrPSc assemblies exhibit a PrPSc subunit as core constituent, which was recently identified. This review summarizes our current knowledge on prion assembly heterogeneity down to the subunit level and will discuss its importance with regard to the current molecular principles of the prion replication process. View Full-Text
Keywords: prion; PrP; amyloid; quasi-species; dynamics prion; PrP; amyloid; quasi-species; dynamics
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

Igel-Egalon, A.; Bohl, J.; Moudjou, M.; Herzog, L.; Reine, F.; Rezaei, H.; Béringue, V. Heterogeneity and Architecture of Pathological Prion Protein Assemblies: Time to Revisit the Molecular Basis of the Prion Replication Process? Viruses 2019, 11, 429.

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]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top