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• Grassmann, A
• Wolf, H
• Hofmann, J
• Graham, J
• Vorberg, I
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• Grassmann, A
• Wolf, H
• Hofmann, J
• Graham, J
• Vorberg, I
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• Grassmann, A
• Wolf, H
• Hofmann, J
• Graham, J
• Vorberg, I

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Viruses 2013, 5(1), 374-405; doi:10.3390/v5010374

Review

Cellular Aspects of Prion Replication In Vitro

Andrea Grassmann ^1,† , Hanna Wolf ^1,† , Julia Hofmann ¹ , James Graham ¹  and Ina Vorberg ^1,2,*

¹ German Center for Neurodegenerative Diseases (DZNE e.V.), Ludwig-Erhard-Allee 2, 53175 Bonn, Germany ² 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; in revised form: 7 January 2013 / Accepted: 16 January 2013 / Published: 22 January 2013

(This article belongs to the Special Issue Recent Developments in the Prion Field)

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Abstract: 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.

Keywords: prion; prion strains; transmissible spongiform encephalopathies; glycosaminoglycans; LRP1; RPSA

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