Ovine recombinant PrP as an inhibitor of ruminant prion propagation in vitro. Issue 4 (4th July 2017)

• Record Type: Journal Article
• Authors: Workman, Rob G.; Maddison, Ben C.; Gough, Kevin C.
• Is Part Of: Prion. Volume 11:Issue 4(2017)
• Page Start: 265
• Page End: 276
• Publication Date: 2017-07-04
• Subjects: BSE -- PMCA -- prion diseases -- protein inhibitors -- recombinant PrP -- Scrapie -- therapeutics; Protein folding -- Periodicals; Prions -- Periodicals; Proteins -- Biotechnology -- Periodicals; 572.633
• DOI: 10.1080/19336896.2017.1342919
• Languages: English
• ISSNs: 1933-6896

Abstract

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.