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Open Access Highly Accessed Research article

In vitro prion protein conversion suggests risk of bighorn sheep (Ovis canadensis) to transmissible spongiform encephalopathies

Aaron R Morawski124, Christina M Carlson23, Haeyoon Chang2 and Christopher J Johnson2*

Author Affiliations

1 Department of Bacteriology, University of Wisconsin, Madison, WI, USA

2 USGS National Wildlife Health Center, Madison, WI, USA

3 Program in Cellular and Molecular Biology, University of Wisconsin, Madison, WI, USA

4 Present address: National Institutes of Health, 9000 Rockville Pike, Bethesda 20892, Maryland, USA

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BMC Veterinary Research 2013, 9:157  doi:10.1186/1746-6148-9-157

Published: 9 August 2013

Additional files

Additional file 1:

Bighorn sheep (BHS) and native host conversion efficiency ratios substrates. Substrates prepared at either pH 7.4 or 3.5 from BHS, mink, domestic sheep or white-tailed deer (WTD) were shaken in the absence of TSE agents. No proteinase K-resistant prion protein was found by immunoblot with monoclonal antibody BAR 224.

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Additional file 2:

Protein misfolding cyclic amplification (PMCA) using domestic sheep (A136R154Q171) genotype substrate. The indicated TSE agents were diluted to 10-2 or 103 from 10% w/v stocks of brain homogenate into domestic sheep PMCA substrate and subjected to 96 cycles of sonication. Proteinase K (PK)-resistant prion protein levels were assessed by immunoblotting with monoclonal antibody BAR 224. As a control, substrate without TSE agent seed was subjected to PMCA cycling. Samples of sheep substrate containing the indicated TSE agents, but not subjected to PMCA, served to establish background levels of PK-resistant prion protein

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