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Protein Folding Activity of the Ribosome (PFAR) –– A Target for Antiprion Compounds
Open AccessArticle

Assessing Proteinase K Resistance of Fish Prion Proteins in a Scrapie-Infected Mouse Neuroblastoma Cell Line

Laboratory for the Research of Neurodegenerative Diseases, Center for Human Genetics, KU Leuven, O&N 4 Herestraat 49, PO Box 602, 3000 Leuven, Belgium
Department of Pharmacy, Aristotle University of Thessaloniki, Thessaloniki GR-54124, Greece
Biological Computation & Process Laboratory (BCPL), Chemical Process Research Institute (CPERI), Centre for Research & Technology (CERTH), PO Box 361, GR-57001 Thessaloniki, Greece
Faculty of Veterinary Medicine, University of Calgary, 2500 University Dr. NW, Calgary, Alberta T2N 1N4, Canada
Author to whom correspondence should be addressed.
Viruses 2014, 6(11), 4398-4421;
Received: 27 August 2014 / Revised: 23 October 2014 / Accepted: 6 November 2014 / Published: 13 November 2014
(This article belongs to the Special Issue Recent Developments in the Prion Field)
The key event in prion pathogenesis is the structural conversion of the normal cellular protein, PrPC, into an aberrant and partially proteinase K resistant isoform, PrPSc. Since the minimum requirement for a prion disease phenotype is the expression of endogenous PrP in the host, species carrying orthologue prion genes, such as fish, could in theory support prion pathogenesis. Our previous work has demonstrated the development of abnormal protein deposition in sea bream brain, following oral challenge of the fish with natural prion infectious material. In this study, we used a prion-infected mouse neuroblastoma cell line for the expression of three different mature fish PrP proteins and the evaluation of the resistance of the exogenously expressed proteins to proteinase K treatment (PK), as an indicator of a possible prion conversion. No evidence of resistance to PK was detected for any of the studied recombinant proteins. Although not indicative of an absolute inability of the fish PrPs to structurally convert to pathogenic isoforms, the absence of PK-resistance may be due to supramolecular and conformational differences between the mammalian and piscine PrPs. View Full-Text
Keywords: prion; fish; cross-species transmission; cell culture; ScN2a prion; fish; cross-species transmission; cell culture; ScN2a
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Salta, E.; Kanata, E.; Ouzounis, C.A.; Gilch, S.; Schätzl, H.; Sklaviadis, T. Assessing Proteinase K Resistance of Fish Prion Proteins in a Scrapie-Infected Mouse Neuroblastoma Cell Line. Viruses 2014, 6, 4398-4421.

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