Next Article in Journal
Airborne Transmission of a Serotype 4 Fowl Adenovirus in Chickens
Next Article in Special Issue
Understanding Prion Strains: Evidence from Studies of the Disease Forms Affecting Humans
Previous Article in Journal
Enhanced Autophagy Contributes to Reduced Viral Infection in Black Flying Fox Cells
Previous Article in Special Issue
Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessReview
Viruses 2019, 11(3), 261; https://doi.org/10.3390/v11030261

Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration

1
Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), 34136 Trieste, Italy
2
Clinical Unit of Neurology, Department of Medicine, Surgery and Health Sciences, University Hospital and Health Services of Trieste, University of Trieste, 34149 Trieste, Italy
3
ELETTRA Sincrotrone Trieste S.C.p.A, Basovizza, 34149 Trieste, Italy
*
Author to whom correspondence should be addressed.
Received: 14 February 2019 / Revised: 8 March 2019 / Accepted: 10 March 2019 / Published: 14 March 2019
(This article belongs to the Special Issue Deciphering the Molecular Targets of Prion and Prion-Like Strains)
  |  
PDF [1203 KB, uploaded 14 March 2019]
  |  

Abstract

Increasing evidence suggests that neurodegenerative disorders share a common pathogenic feature: the presence of deposits of misfolded proteins with altered physicochemical properties in the Central Nervous System. Despite a lack of infectivity, experimental data show that the replication and propagation of neurodegenerative disease-related proteins including amyloid-β (Aβ), tau, α-synuclein and the transactive response DNA-binding protein of 43 kDa (TDP-43) share a similar pathological mechanism with prions. These observations have led to the terminology of “prion-like” to distinguish between conditions with noninfectious characteristics but similarities with the prion replication and propagation process. Prions are considered to adapt their conformation to changes in the context of the environment of replication. This process is known as either prion selection or adaptation, where a distinct conformer present in the initial prion population with higher propensity to propagate in the new environment is able to prevail over the others during the replication process. In the last years, many studies have shown that prion-like proteins share not only the prion replication paradigm but also the specific ability to aggregate in different conformations, i.e., strains, with relevant clinical, diagnostic and therapeutic implications. This review focuses on the molecular basis of the strain phenomenon in prion and prion-like proteins. View Full-Text
Keywords: prion; prion-like proteins; strains; neurodegeneration prion; prion-like proteins; strains; neurodegeneration
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

Scialò, C.; De Cecco, E.; Manganotti, P.; Legname, G. Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration. Viruses 2019, 11, 261.

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