Chronic Wasting Disease Prions in Elk Antler Velvet
Rachel C. Angers1, Tanya S. Seward, Dana Napier, Michael Green, Edward Hoover, Terry Spraker, Katherine O’Rourke, Aru Balachandran, and Glenn C. Telling
Author affiliations: University of Kentucky Medical Center, Lexington, Kentucky, USA (R.C. Angers, T.S. Seward, D. Napier, M. Green, G.C. Telling); Colorado State University, Fort Collins, Colorado, USA (E. Hoover, T. Spraker); US Department of Agriculture, Pullman, Washington, USA (K. O’Rourke); Canadian Food Inspection Agency, Ottawa, Ontario, Canada (A. Balachandran); 1Current affiliation: Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Figure 6. Detection of CerPrPSc (disease-associated form of cervid prion protein [PrP]) in brain and antler velvet from chronic wasting disease (CWD)–affected elk after serial protein misfolding cyclic amplification (PMCA). Western blots demonstrate amplification of protease-resistant prion protein (PrP) after serial PMCA when seeded with brain or velvet antler material from CWD-affected elk. Brain samples: lane 1, Tg(CerPrP)1536+/– brain material not treated with proteinase K (PK); lane 2, Tg(CerPrP)1536+/– brain material used as a negative control seed for the PMCA reactions; lanes 3–9, 10–2 to 10–8 dilutions of 10% elk brain homogenate. Antler velvet samples: lane 1, Tg(CerPrP)1536+/– brain material not treated with PK; lane 2, Tg(CerPrP)1536+/– brain material used as a negative control seed for the PMCA reactions; lanes 3–9, replicate 10–2 dilutions of 10% antler velvet homogenate. Samples were either treated or not treated with PK as indicated. Membranes were probed with monoclonal antibody 6H4. Tg, transgenic.
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