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Presence and Seeding Activity of Pathological Prion Protein (PrPTSE) in Skeletal Muscles of White-Tailed Deer Infected with Chronic Wasting Disease

By Martin L. Daus, Johanna Breyer, Katja Wagenfuehr, Wiebke M. Wemheuer, Achim Thomzig, Walter J. Schulz-Schaeffer and Michael Beekes


Chronic wasting disease (CWD) is a contagious, rapidly spreading transmissible spongiform encephalopathy (TSE), or prion disease, occurring in cervids such as white tailed-deer (WTD), mule deer or elk in North America. Despite efficient horizontal transmission of CWD among cervids natural transmission of the disease to other species has not yet been observed. Here, we report for the first time a direct biochemical demonstration of pathological prion protein PrPTSE and of PrPTSE-associated seeding activity, the static and dynamic biochemical markers for biological prion infectivity, respectively, in skeletal muscles of CWD-infected cervids, i. e. WTD for which no clinical signs of CWD had been recognized. The presence of PrPTSE was detected by Western- and postfixed frozen tissue blotting, while the seeding activity of PrPTSE was revealed by protein misfolding cyclic amplification (PMCA). Semi-quantitative Western blotting indicated that the concentration of PrPTSE in skeletal muscles of CWD-infected WTD was approximately 2000-10000 -fold lower than in brain tissue. Tissue-blot-analyses revealed that PrPTSE was located in muscle-associated nerve fascicles but not, in detectable amounts, in myocytes. The presence and seeding activity of PrPTSE in skeletal muscle from CWD-infected cervids suggests prevention of such tissue in the human diet as a precautionary measure for food safety, pending on further clarification of whether CWD may be transmissible to humans

Topics: Research Article
Publisher: Public Library of Science
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Provided by: PubMed Central

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  1. (1993). A kinetic model for amyloid formation in the prion diseases: importance of seeding.
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  6. (2005). Chronic wasting disease.
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  10. (2010). Experimental oral transmission of chronic wasting disease to red deer (Cervus elaphus elaphus): early detection and late stage distribution of proteaseresistant prion protein.
  11. (2008). Experimental transmission of chronic wasting disease (CWD) of elk (Cervus elaphus nelsoni), white-tailed deer (Odocoileus virginianus), and mule deer (Odocoileus hemionus hemionus) to white-tailed deer by intracerebral route.
  12. (2004). Failure to detect prion protein (PrPres) by immunohistochemistry in striated muscle tissues of animals experimentally inoculated with agents of transmissible spongiform encephalopathy.
  13. (1982). Novel proteinaceous infectious particles cause scrapie.
  14. (2006). Pathological prion protein in muscles of hamsters and mice infected with rodentadapted BSE or vCJD.
  15. (2004). Preclinical deposition of pathological prion protein PrPSc in muscles of hamsters orally exposed to scrapie.
  16. (2006). Prion protein in cardiac muscle of elk (Cervus elaphus nelsoni) and white-tailed deer (Odocoileus virginianus) infected with chronic wasting disease.
  17. (2010). Prion strain mutation determined by prion protein conformational compatibility and primary structure.
  18. (2002). Prions in skeletal muscle.
  19. (2006). Prions in skeletal muscles of deer with chronic wasting disease.
  20. (2009). Prions: protein aggregation and infectious diseases.
  21. (1998). Prions.
  22. (2004). PrPSc accumulation in myocytes from sheep incubating natural scrapie.
  23. (2005). PrPTSE distribution in a primate model of variant, sporadic, and iatrogenic Creutzfeldt-Jakob disease.
  24. (2007). Scrapie Agent (Strain 263K) can transmit disease via the oral route after persistence in soil over years.
  25. (1997). Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.
  26. (2009). Susceptibilities of nonhuman primates to chronic wasting disease.
  27. (2000). The paraffin-embedded tissue blot detects PrP(Sc) early in the incubation time in prion diseases.
  28. (2007). The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies.
  29. (2007). Transmission and adaptation of chronic wasting disease to hamsters and transgenic mice: evidence for strains.
  30. (2007). Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein.
  31. (1995). Western blot mapping of disease-specific amyloid in various animal species and humans with transmissible spongiform encephalopathies using a high-yield purification method.
  32. (2003). Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie.