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Ovine recombinant PrP as an inhibitor of ruminant prion propagation in vitro

Maddison, Ben C.; Workman, Robert G.; Gough, Kevin C.

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Authors

Ben C. Maddison

Robert G. Workman

Kevin C. Gough



Abstract

Prion diseases are fatal and incurable neurodegenerative diseases of humans and animals. Despite years of research, no therapeutic agents have been developed that can effectively manage or reverse disease progression. Recently it has been identified that recombinant prion proteins (rPrP) expressed in bacteria can act as inhibitors of prion replication within the in vitro prion replication system Protein Misfolding Cyclic Amplification (PMCA). Here, within PMCA reactions amplifying a range of ruminant prions including distinct Prnp genotypes/host species and distinct prion strains, recombinant ovine VRQ PrP displayed consistent inhibition of prion replication and produced IC50 values of 122 and 171 nM for ovine scrapie and bovine BSE replication, respectively. These findings illustrate the therapeutic potential of rPrPs with distinct TSE diseases.

Journal Article Type Article
Acceptance Date Jun 12, 2017
Online Publication Date Jun 30, 2017
Deposit Date Jun 21, 2017
Publicly Available Date Jun 30, 2017
Journal Prion
Print ISSN 1933-6896
Electronic ISSN 1933-690X
Publisher Taylor & Francis Open
Peer Reviewed Peer Reviewed
Volume 11
Issue 4
DOI https://doi.org/10.1080/19336896.2017.1342919
Keywords Scrapie, BSE, Recombinant PrP, prion diseases, PMCA, Protein inhibitors, Therapeutics
Public URL https://nottingham-repository.worktribe.com/output/870614
Publisher URL http://www.tandfonline.com/doi/full/10.1080/19336896.2017.1342919

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