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Commentary

Open Access

Zombie deer and the species barrier. Should humans worry about it?

  • Joseph V. Pergolizzi1
  • Giustino Varrassi2
  • Jo Ann LeQuang1

1NEMA Research, Inc., Naples, Florida, United States of America

2Paolo Procacci Foundation, via Tacito 7, 00193 Roma, Italy

DOI: 10.22514/sv.2020.16.0092

Online publish date: 17 November 2020

*Corresponding Author(s): Jo Ann LeQuang E-mail: joannlequang@gmail.com

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Abstract

This commentary reports of a deer chronic disease (chronic wasting disease - CWD), which might be transmitted to humans. It is due to a prion infection, similar to the bovine spongiform encephalopathy (BSE). At the moment, it is not known if the disease may be transmitted to humans. That is why all of us should be aware of the disease, and more careful while consuming deer meat.

Key words

Chronic wasting disease (CWD); transmissible diseases; prions; spongiform en-cephalopathy

Cite And Share

Joseph V. Pergolizzi,Giustino Varrassi,Jo Ann LeQuang. Zombie deer and the species barrier. Should humans worry about it?. Signa Vitae. 2020.doi:10.22514/sv.2020.16.0092.

References

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[2] Williams E, Miller M. Chronic wasting disease in deer and elk in North America. Revue Scientifique et Technique. 2002; 21: 305-316.

[3] Belay E, Maddox R, Williams E, Miller M, Gambetti P, Schonberger L. Chronic wasting disease and potential transmission to humans. Emerging Infectious Diseases. 2004; 10: 977-984.

[4] Saunders SE, Bartelt-Hunt SL, Bartz JC. Occurrence, transmission, and zoonotic potential of chronic wasting disease. Emerging Infectious Diseases. 2012; 18: 369-376.

[5] Jennelle CS, Samuel MD, Nolden CA, Keane DP, Barr DJ, Johnson C, et al. Surveillance for transmissible spongiform encephalopathy in scavengers of white-tailed deer carcasses in the chronic wasting disease area of Wisconsin. Journal of Toxicology and Environmental Health, Part A. 2009; 72: 1018-1024.

[6] Igel-Egalon A, Laferrière F, Tixador P, Moudjou M, Herzog L, Reine F, et al. Crossing species barriers relies on structurally distinct prion assemblies and their complementation. Molecular Neurobiology. 2020; 57: 2572-2587.

[7] Hosszu LLP, Conners R, Sangar D, Batchelor M, Sawyer EB, Fisher S, et al. Structural effects of the highly protective V127 polymorphism on human prion protein. Communications Biology. 2020; 3: 402.

[8] Sharma A, Bruce KL, Chen B, Gyoneva S, Behrens SH, Bommarius AS, et al. Contributions of the prion protein sequence, strain, and environment to the species barrier. Journal of Biological Chemistry. 2016; 291: 1277-1288.

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