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Chronic wasting disease (CWD) has recently emerged in North America as an important prion disease of captive and free-ranging cervids (species in the deer family). CWD is the only recognized transmissible spongiform encephalopathy (TSE) affecting free-ranging species. ...CWD has also infected farmed cervids in numerous jurisdictions, and has probably been endemic in North America's farmed deer and elk for well over a decade. Several free-ranging foci distant to the Colorado-Wyoming core area have been discovered since 2000, and new or intensified surveillance may well identify even more foci of infection. ...CWD is infectious, transmitting horizontally from infected to susceptible cervids. Early accumulation of PrP(CWD) in alimentary tract-associated lymphoid tissues during incubation suggests agent shedding in feces or saliva as plausible transmission routes. Residual infectivity in contaminated environments also appears to be important in sustaining epidemics. Improved tests allow CWD to be reliably diagnosed long before clinical signs appear. ...Although recognized as a transmissible spongiform encephalopathy (TSE) since the late 1970s (Williams and Young 1980, 1982), interest in and concern about CWD has only recently emerged. ...The geographic extent of endemic CWD in free-ranging wildlife was initially thought to be quite limited and its natural rate of expansion slow; however, recent investigations have revealed that CWD has been inadvertently spread much more widely via market-driven movements of infected, farmed elk and deer. Both the ecological and economic consequences of CWD and its spread remain to be determined; moreover, public health implications remain a question of intense interest.
"Cross-species infection with transmissible spongiform encephalopathy agents may lead to subclinical infection and to adaptation of the infection to new species."
* "Subclinical scrapie infection in a resistant species: persistence, replication, and adaptation of infectivity during four passages." Race R, Meade-White K, Raines A, Raymond GJ, Caughey B, Chesebro B. Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, 903 S. Fourth Street, Hamilton, MT 59840, USA. J Infect Dis. 2002 Dec 1;186 Suppl 2:S166-70. PMID: 12424693
"...prions may overcome natural transmissibility barriers between two species of mammals. This may happen if prion proteins from one of these two species have been exposed to abnormal prions from a third species."
* "Researchers Make Major Gain In Understanding How Prions Jump Species" Source: Case Western Reserve University
"Conformational variations in an infectious protein determine prion strain differences." Nature. 2004 Mar 18;428(6980):323-8. Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94143, USA. PMID: 15029196
"...the (prion strain) biochemical isoform of PrP(Sc) found is influenced by the cell type in which it accumulates."
* "Peripheral Tissue Involvement in Sporadic, Iatrogenic, and Variant Creutzfeldt-Jakob Disease: An Immunohistochemical, Quantitative, and Biochemical Study." Am J Pathol. 2004 Jan;164(1):143-153. Head MW, Ritchie D, Smith N, McLoughlin V, Nailon W, Samad S, Masson S, Bishop M, McCardle L, Ironside JW. National Creutzfeldt-Jakob Disease Surveillance Unit and Division of Pathology, School of Molecular and Clinical Medicine, University of Edinburgh, Western General Hospital, Edinburgh, United Kingdom. PMID: 14695328
Also see: "Mad Cow" Disease Uses Immune System to Spread in Body
Prion researchers say underlying "subclinical" prion infections cause disease well before the infection moves to the brain; there is a progressive, degenerative disease process affecting various body parts and systems.
"Diverse human disorders …arise from misfolding and aggregation of an underlying protein."
"Protein misfolding and disease: the case of prion disorders." Cell Mol Life Sci. 2003 Jan;60(1):133-43. Hetz C, Soto C. Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan les Ouates, Switzerland. PMID: 12613663
* "Chronic Subclinical Prion Disease Induced by Low-Dose Inoculum" Received September 24, 2001; J Virol. 2002 March; 76 (5): 2510–2517 Alana M. Thackray,1 Michael A. Klein,2 Adriano Aguzzi,3 and Raymond Bujdoso www.pubmedcentral.nih.gov...
"Subclinical prion infection in humans and animals." Br Med Bull. 2003;66:161-70. Hill AF, Collinge J. MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, London, UK. PMID: 14522857
"How does chronic wasting disease (CWD) in deer and elk spread from animal to animal? … University of Wisconsin-Madison researchers show that prions - infectious proteins considered to be at the root of the disease - literally stick to some soil types, suggesting that the landscape may serve as an environmental reservoir for the disease."
* Prion transmission in blood and urine: what are the implications for recombinant and urinary-derived gonadotrophins? Hum Reprod. 2002 Oct;17(10):2501-8. Reichl H, Balen A, Jansen CA. PMID: 12351519
"This finding indicates that previous attempts to quantify BSE and scrapie prions in milk or non-neural tissues, such as muscle, may have underestimated infectious titers by as much as a factor of 10,000, raising the possibility that prions could be present in these products in sufficient quantities to pose risk to humans..."
* UCSF-Led Team Reports New Test Improves Detection of Prions in Animals
"It is possible that infectious prions have leached into the water supply, government scientists admit. … The main risks to human health are contamination of water supplies from buried animals, or carcasses awaiting disposal, and pollution of the air from burning pyres."
"Fly larvae and mites were exposed to brain-infected material and were readily able to transmit scrapie (prions) to hamsters. New lines of evidence have confirmed that adult flies are also able to express prion proteins. Several cell types found on the human skin, including keratinocytes, fibroblasts and lymphocytes, are susceptible to the abnormal infective isoform of the prion protein, which transforms the skin to produce a potential target for prion infection."
* Could ectoparasites act as vectors for prion diseases? Int J Dermatol. 2003 Jun;42(6):425-9. Lupi O. Center for Vaccine Development, University of Texas Medical Branch at Galveston, Galveston, TX, USA. PMID: 12786866
This 1986 paper describes how "proteinaceous capsids" use viruses as vehicles of transmission, and how the subsequent RNA interference silences genes.
* "Viral influences on aflatoxin formation by Aspergillus flavus." Appl Microbiol Biotechnol 24:248-252. Schmidt FR, Lemke PA, Esser K (1986)
"Epidemiological observations indicate that a microbial vector is responsible for the transmission of natural prion disease in sheep and goats … A similar phenomenon was already described with a protein antigen of the ameba Naegleria gruberi. ...It is proposed that many microbial proteins may be capable of replicating themselves in mammalian cells eliciting and sustaining thereby degenerative and/or autoimmune reactions subsequent to infections with microorganisms."
* Med Hypotheses. 1999 Aug;53(2):91-102. Is the pathogen of prion disease a microbial protein? Fuzi M. Budapest Institute of National Public Health and Medical Officer Service, Hungary. PMID: 10532698
"Although composting reaches high enough temperatures for a long enough time to kill most pathogens ...it would be highly unlikely that composting would inactivate prions."
Originally posted by DrHoracid
How did the prions cross over? Last time I checked deer and elk were not "carnivores". Was if from "deerhunter" feeding at the deer stands? Or was there something else. Perhaps a bioresearch lab located at the heart of the infected area? Poor biowaste control?
Originally posted by justme1640
there was a theory that elk and deer had jumped fences and possibly eaten cow feed that was infected
just waiting for the fish wasting disease.
You absolutely CANNOT allow any meat infected with these diseases enter your system whatsoever, no matter what "precautions" you take, because there are none to be taken in the preparation of the contaminated product.
Originally posted by Ghaleon4
You don't "kill" a Prion...it's not a living organism. It's a mis-folded protein...when you cook meat, and eat it, you're still getting "protein". Inluding the prions. Doesn't matter how well you cook the stuff...I VERY loosely think of it as kind of like eating meat with fiberglass in it (might be a bad example, but...). No matter how much you cook it, the fiberglass will still be in there. When you eat it, the fiberglass then gets caught up in your stomach, you develop diseases/cancer in your digestive system as a result. Prions are similar, only of course the symptoms are based around the nervous system. The developing proteins in your body come into contact with these "Misbehaved" proteins, and become dilinquent themselves...
Thorough cooking is not going to help anyone here. You absolutely CANNOT allow any meat infected with these diseases enter your system whatsoever, no matter what "precautions" you take, because there are none to be taken in the preparation of the contaminated product.
You have voted soficrow for the Way Above Top Secret award.
Originally posted by DontTreadOnMe
You have voted soficrow for the Way Above Top Secret award.
Sofi, many thanks for keeping the ATS community aware and informed on this potentially human illness.
What am I missing? What technology are we not using to cotain or prevent this disease from spreading?