Next Article in Journal
Apoptosis in Pneumovirus Infection
Next Article in Special Issue
Low Copper and High Manganese Levels in Prion Protein Plaques
Previous Article in Journal
Influenza A Virus Entry Inhibitors Targeting the Hemagglutinin
Previous Article in Special Issue
Prion Disease and the Innate Immune System
Article Menu

Export Article

Open AccessReview
Viruses 2013, 5(1), 374-405;

Cellular Aspects of Prion Replication In Vitro

German Center for Neurodegenerative Diseases (DZNE e.V.), Ludwig-Erhard-Allee 2, 53175 Bonn, Germany
Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Received: 12 December 2012 / Revised: 7 January 2013 / Accepted: 16 January 2013 / Published: 22 January 2013
(This article belongs to the Special Issue Recent Developments in the Prion Field)
Full-Text   |   PDF [753 KB, uploaded 12 May 2015]   |  


Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders in mammals that are caused by unconventional agents predominantly composed of aggregated misfolded prion protein (PrP). Prions self-propagate by recruitment of host-encoded PrP into highly ordered b-sheet rich aggregates. Prion strains differ in their clinical, pathological and biochemical characteristics and are likely to be the consequence of distinct abnormal prion protein conformers that stably replicate their alternate states in the host cell. Understanding prion cell biology is fundamental for identifying potential drug targets for disease intervention. The development of permissive cell culture models has greatly enhanced our knowledge on entry, propagation and dissemination of TSE agents. However, despite extensive research, the precise mechanism of prion infection and potential strain effects remain enigmatic. This review summarizes our current knowledge of the cell biology and propagation of prions derived from cell culture experiments. We discuss recent findings on the trafficking of cellular and pathologic PrP, the potential sites of abnormal prion protein synthesis and potential co-factors involved in prion entry and propagation. View Full-Text
Keywords: prion; prion strains; transmissible spongiform encephalopathies; glycosaminoglycans; LRP1; RPSA prion; prion strains; transmissible spongiform encephalopathies; glycosaminoglycans; LRP1; RPSA

Figure 1

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Share & Cite This Article

MDPI and ACS Style

Grassmann, A.; Wolf, H.; Hofmann, J.; Graham, J.; Vorberg, I. Cellular Aspects of Prion Replication In Vitro. Viruses 2013, 5, 374-405.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



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