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Pathogens 2017, 6(4), 67; https://doi.org/10.3390/pathogens6040067

Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies

1
CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Spain
2
IKERBASQUE, Basque Foundation for Science, 48011 Bilbao, Spain
*
Author to whom correspondence should be addressed.
Received: 25 October 2017 / Revised: 8 December 2017 / Accepted: 12 December 2017 / Published: 14 December 2017
(This article belongs to the Special Issue PrPSc prions: state of the art)
Full-Text   |   PDF [309 KB, uploaded 14 December 2017]

Abstract

The misfolding of the cellular prion protein (PrPC) into the disease-associated isoform (PrPSc) and its accumulation as amyloid fibrils in the central nervous system is one of the central events in transmissible spongiform encephalopathies (TSEs). Due to the proteinaceous nature of the causal agent the molecular mechanisms of misfolding, interspecies transmission, neurotoxicity and strain phenomenon remain mostly ill-defined or unknown. Significant advances were made using in vivo and in cellula models, but the limitations of these, primarily due to their inherent complexity and the small amounts of PrPSc that can be obtained, gave rise to the necessity of new model systems. The production of recombinant PrP using E. coli and subsequent induction of misfolding to the aberrant isoform using different techniques paved the way for the development of cell-free systems that complement the previous models. The generation of the first infectious recombinant prion proteins with identical properties of brain-derived PrPSc increased the value of cell-free systems for research on TSEs. The versatility and ease of implementation of these models have made them invaluable for the study of the molecular mechanisms of prion formation and propagation, and have enabled improvements in diagnosis, high-throughput screening of putative anti-prion compounds and the design of novel therapeutic strategies. Here, we provide an overview of the resultant advances in the prion field due to the development of recombinant PrP and its use in cell-free systems. View Full-Text
Keywords: Prion disease; TSE; recombinant PrP; in vitro propagation; PMCA; QuIC Prion disease; TSE; recombinant PrP; in vitro propagation; PMCA; QuIC
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).
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Charco, J.M.; Eraña, H.; Venegas, V.; García-Martínez, S.; López-Moreno, R.; González-Miranda, E.; Pérez-Castro, M.Á.; Castilla, J. Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies. Pathogens 2017, 6, 67.

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