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South Dakota Begins Another Round of CWD Testing

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South Dakota Begins Another Round of CWD Testing

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Posts: 230
South Dakota Begins Another Round of CWD Testing

Chronic wasting persists in Hills
Seven deer, four elk found to have chronic wasting disease.
By The Associated Press

PIERRE -- Seven deer and four elk were found to have chronic wasting disease
from 2,539 samples in the most recent testing done for the state Department
of Game, Fish & Parks.

All of the infected animals were from Custer, Fall River and Pennington
counties in southwest South Dakota -- the location of all previous CWD cases
in the wild.

Chronic wasting disease attacks the brain in deer and elk and is always
fatal. It's been found in the wild in more than a half-dozen states.

Researchers test for the disease from samples submitted by hunters and from
sick animals observed in the wild.

The positive cases in the July 1, 2006 to June 30, 2007 period included two
elk from Custer State Park and an elk from Wind Cave National Park.

Samples also were taken in the past year from deer killed by hunters in
Grant and Deuel counties in eastern South Dakota. Those counties were added
to the surveillance plan because a CWD-infected deer was discovered at a
farm in Minnesota.

The GF&P said testing will again be done on elk and deer taken by hunters
this fall in the Black Hills and Fall River, Custer, Pennington, Deuel and
Grant counties.

Thirty-nine cases of CWD have been found in deer and 19 in elk from the
18,846 samples tested in South Dakota since 1997, the GF&P said. Seventeen
of the infected animals came from Wind Cave National Park.

http://www.rapidcityjournal.com/articles/2007/10/09/news/top/doc470bba9f...

Maps Showing Locations of Positive CWD Tests

http://www.sdgfp.info/Wildlife/hunting/BigGame/SDakota06-07.jpg
Map of CWD Positives in S.D. 2006 - June 2007
http://www.sdgfp.info/Wildlife/hunting/BigGame/SDakota01-07.jpg
Statewide View of Positive CWD Cases 2001 - June 2007
http://www.sdgfp.info/Wildlife/hunting/BigGame/Hills06-07.jpg
Map of CWD Positives in Black Hills 2006 to June 2007
http://www.sdgfp.info/Wildlife/hunting/BigGame/Hills01-07.jpg
Black Hills View of Positive CWD Cases 2001 - June 2007

From: "Terry S. Singeltary Sr."
Subject: CWD UPDATE 88 AUGUST 31, 2007

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0709&L=sanet-mg&T=0&P=450

Date: Wed, 29 Aug 2007 21:13:08 -0500
From: "Terry S. Singeltary Sr."
Subject: CWD NEW MEXICO RECORDS IT'S 19 CASE (near Texas border again)

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0708&L=sanet-mg&T=0&P=26079

Monitoring the Potential Transmission of Chronic Wasting Disease to Humans
Using a Hunter Registry Database in Wyoming (405 lines)
From: Terry S. Singeltary Sr.
Date: Thu, 30 Aug 2007 21:23:42 -0500

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0708&L=sanet-mg&T=0&F=&S=...

Subject: Cross-sequence transmission of sporadic Creutzfeldt-Jakob disease
creates a new prion strain

Date: August 25, 2007 at 12:42 pm PST

Subject: Cross-sequence transmission of sporadic Creutzfeldt-Jakob disease
creates a new prion strain
Date: August 25, 2007 at 12:42 pm PST

J Biol Chem. 2007 Aug 20; : 17709374

Cross-sequence transmission of sporadic Creutzfeldt-Jakob disease creates a
new prion strain.

[My paper] Atsushi Kobayashi , Masahiro Asano , Shirou Mohri , Tetsuyuki
Kitamoto

The genotype (methionine or valine) at polymorphic codon 129 of the human
prion protein (PrP) gene and the type (type 1 or type 2) of abnormal isoform
of PrP (PrP(Sc)) are major determinants of the clinicopathological
phenotypes of sporadic Creutzfeldt-Jakob disease (sCJD). Here we found that
transmission of sCJD prions from a patient with valine homozygosity (129V/V)
and type 2 PrP(Sc) (sCJD-VV2 prions) to mice expressing human PrP with
methionine homozygosity (129M/M) generated unusual PrP(Sc) intermediate in
size between type 1 and type 2. The intermediate type PrP(Sc) was seen in
all examined dura mater graft-associated CJD cases with 129M/M and
plaque-type PrP deposits (p-dCJD). p-dCJD prions and sCJD-VV2 prions
exhibited similar transmissibility and neuropathology, and the identical
type of PrP(Sc) when inoculated into PrP-humanized mice with 129M/M or
129V/V. These findings suggest that p-dCJD could be caused by cross-sequence
transmission of sCJD-VV2 prions.

snip...

In this study, the strain-dependent traits of sCJDMM1
prions were inherited through cross-sequence
transmission without any modification. The
humanized mice with 129V/V produced type 1 PrPres
after inoculation with sCJD-MM1 prions. Because
sCJD-VV1 cases are extremely rare (at most 1-2%
of the total number of sCJD cases) and characterized
by early onset (mean age at onset: 39.3 years) (5),

####################################

our results raise the possibility that CJD cases
classified as VV1 may include cases caused by
iatrogenic transmission of sCJD-MM1 prions or
food-borne infection by type 1 prions from animals,
e.g., chronic wasting disease prions in cervid. In fact,
two CJD-VV1 patients who hunted deer or
consumed venison have been reported (40, 41). The
results of the present study emphasize the need for
traceback studies and careful re-examination of the
biochemical properties of sCJD-VV1 prions.

###################################

In conclusion, cross-sequence transmission of
sCJD-VV2 prions generates a new prion strain with
altered conformational properties and disease
phenotypes as p-dCJD prions. Furthermore, the
newly generated prions have unique transmissibility
including the traceback phenomenon. In the future, if
atypical prion strains emerge through cross-sequence
transmission, especially from animals, traceback
studies will enable us to identify the origin of the
prions.

REFERENCES...snip...end

FULL TEXT ;

http://www.jbc.org/cgi/content/abstract/M704597200v1?maxtoshow=&HITS=10&...

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0708&L=sanet-mg&T=0&P=21267

Re: Colorado Surveillance Program for Chronic Wasting Disease
Transmission to Humans (TWO SUSPECT CASES)

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0704&L=sanet-mg&T=0&P=1165

Subject: MAD COW BASE H-TYPE AND L-TYPE

Date: August 23, 2007 at 11:30 am PST

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0708&L=sanet-mg&T=0&P=19779

CWD

http://savannahnow.com/node/366050

Terry S. Singeltary Sr.
P.O. Box 42
Bacliff, Texas USA 77518

Offline
Joined: 01/01/2006
Posts: 230
South Dakota Begins Another Round of CWD Testing

P04.61

Survival of PrPSc during Simulated Wastewater Treatment Processes

Pedersen, J1; Hinckley, G1; McMahon, K2; McKenzie, D3; Aiken, JM3 1University of Wisconsin, Soil Science/Civil and Environmental Engineering, USA; 2University of Wisconsin, Civil and Environmental Engineering, USA; 3University of Wisconsin, Comparative Biosciences, USA

Concern has been expressed that prions could enter wastewater treatment systems through sewer and/or septic systems (e.g., necropsy laboratories, rural meat processors, private game dressing) or through leachate from landfills that have received TSE-contaminated material. Prions are highly resistant to degradation and many disinfection procedures raising concern that they could survive conventional wastewater treatment. Here, we report the results of experiments examining the partitioning and survival of PrPSc during simulated wastewater treatment processes including activated and mesophilic anaerobic sludge digestion. We establish that PrPSc can be efficiently extracted from activated and anaerobic digester sludges with 1% sodium dodecyl sulfate, 10% sodium undecyl sulfate, and 1% sodium N-lauryl sarcosinate. Activated sludge digestion does not result in significant degradation of PrPSc. The protein partitions strongly to the activated sludge solids and is expected to enter biosolids treatment processes. A large fraction of PrPSc survived simulated mesophilic anaerobic sludge digestion. Our results suggest that if prions were to enter municipal waste water treatment systems, most of the agent would partition to activated sludge solids, survive mesophilic anaerobic digestion, and be present in treated biosolids. Land application of biosolids containing prions could represent a route for their unintentional introduction into the environment. Our results argue for excluding inputs of prions to municipal wastewater treatment facilities that would result in unacceptable risk of prion disease transmission via contaminated biosolids.

http://www.prion2007.com/pdf/Prion%20Book%20of%20Abstracts.pdf

P04.01

Chronic Wasting Disease in a Captive White-Tailed Deer Farm

Keane, D1; Barr, D1; Bochsler, P1; Hall, M2; Gidlewski, T3; O'Rourke, K4; Spraker, T5 1University of Wisconsin, USA; 2US Department of Agriculture, USA; 3US Department of Agriculture, USA; 4USDA ARS-ADRU, Washington |State University, USA; 5Veterinary Diagnostic Laboratory, Colorado State University, USA

A white-tailed deer farm in Portage, Wisconsin, was depopulated in January 2006, after chronic wasting disease (CWD) had been initially discovered on the property in September 2002. Prior to the depopulation, a total of 22 positive animals had been removed from the property: one in 2002, six in 2003, ten in 2004, four in 2005 and one in 2006. At the time of depopulation a total of 76 animals remained: 47 females and 29 males. Age was assessed by visual examination of teeth at the time of death and revealed 26 adult, 8 fawn and 42 yearling animals. The following tissues were examined by immunohistochemistry for PrPCWD using Ab99/97.6.1: obex, tonsil, retropharyngeal, submandibular, parotid, prescapular, axillary, inguinal, prefemoral and popliteal lymph nodes, recto-anal mucosal tissue and eye. Seventy-nine percent of animals (sixty) were found to be positive in at least one tissue; 49 were obex positive, 58 retropharyngeal positive, 56 tonsil positive, 48 recto-anal mucosal associated lymphoid tissue positive and 4 animals were positive for PrPCWD in the retina. Prion genotype was determined for all animals.

http://www.prion2007.com/pdf/Prion%20Book%20of%20Abstracts.pdf

P01.47

Quantifying the Species Barrier in Chronic Wasting Disease by a Novel in vitro Conversion Assay

Li, L1; Coulthart, MB2; Balachandran, A3; Chakrabartty, A4; Cashman, NR1 1University of British Columbia, Brain Research Centre, Canada; 2Public Health Agency of Canada, National Microbiology Laboratory, Canada; 3Animal Diseases Research Institute, Canada Food Inspection Agency, National Reference Laboratory for Scrapie and CWD, Canada; 4Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Canada

Background: Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy that can affect North American cervids (deer, elk, and moose). Although the risk of CWD crossing the species barrier and causing human disease is still unknown, however, definite bovine spongiform encephalopathy (BSE) transmission to humans as variant CJD (vCJD), it would seem prudent to limit the exposure of humans to CWD.

Aim: In view of the fact that BSE can be readily transmitted to non-bovid species, it is important to establish the species susceptibility range of CWD.

Methods: In vitro conversion system was performed by incubation of prions with normal brain homogenates as described before, and protease K (PK) resistant PrP was determined by immunoblotting with 6H4 monoclonal prion antibody.

Results: Our results demonstrate that PrPC from cervids (including moose) can be efficiently converted to a protease-resistant form by incubation with elk CWD prions, presumably due to sequence and structural similarities between these species. Interestingly, hamster shows a high conversion ratio by PrPCWD. Moreover, partial denaturation of substrate PrPC can apparently overcome the structural barriers between more distant species.

Conclusions: Our work correctly predicted the transmission of CWD to a wild moose. We find a species barrier for prion protein conversion between cervids and other species, however, this barrier might be overcome if the PrPC substrate has been partially denatured in a cellular environment. Such an environment might also promote CWD transmission to non-cervid species, *** including humans. Acid/GdnHCl-treated brain PrPC was a superior substrate for the in vitro conversion than PrPC treated at physiological pH. This has implications for the process by which the prion protein is converted in disease.

http://www.prion2007.com/pdf/Prion%20Book%20of%20Abstracts.pdf

Subject: Clinical Observations of BSE Infection in Red Deer Date: October 4, 2007 at 9:05 am PST

P04.80

Clinical Observations of BSE Infection in Red Deer

Steele, P1; Martin, S2; Jeffrey, M2; González, L2; Sisó, S2; Finlayson, J1; Hamilton, S1; Eaton, Samatha L1; Reid, Hugh W1; Todd, R1; Pang, Y1; Chianini, F1; Dagleish, MP1 1Moredun Research Institute, UK; 2Veterinary Laboratory Agency, Lasswade, UK

Observation of clinical signs is often the first step in the diagnosis of TSE diseases in experimental, farmed and wild animals. Clinical presentation of chronic wasting disease (CWD) infected deer varies widely as disease progresses and many clinical signs observed can be non-specific to TSE infection, however by terminal stage the majority of cases involve behavioural changes and loss of body condition. We present here the first description of clinical disease in deer experimentally infected with BSE. These data are part of the results of an ongoing project to investigate the susceptibility of UK red deer (Cervus elaphus elaphus) to BSE infection either by alimentary or intra-cerebral infection. Eighteen European red deer calves (mean 64 days old) were challenged intragastrically with 25g of BSE-infected bovine brain. Six challenged and 2 control deer were culled at 6 and 12 month post infection. These animals showed no clinical signs and no disease-specific PrP (PrPd) on immunohistochemistry (IHC) examination of a wide range of tissues collected at post-mortem. Six BSE-dosed and 4 negative control deer are still alive at time of writing (1384 dpi). Subsequently, 6 red deer of the same cohort (mean 341 days old) were challenged with 0.05g of BSE positive bovine brain material and 2 with sterile saline by the intracerebral route. Currently (1106 dpi), five of the six challenged animals have developed clinical signs and terminal disease confirmed by IHC and western blot detection of PrPd. Clinical signs similar to CWD cases have been observed including behavioral change, wide stance, lowered head, and excessive salivation. All animals had significant weight loss attributed to inability or unwillingness to feed, with inhalation pneumonia occurring in the case of one animal which is commonly observed in CWD cases. The first animal to show clinical signs was markedly different to the four subsequent cases. This animal had to be culled following several behavioral episodes causing physical injury. Our results prove for the first time that UK red deer are susceptible to intra-cerebral BSE infection and shows that the clinical presentation of disease shares many similarities to that recorded for CWD.

http://www.prion2007.com/pdf/Prion%20Book%20of%20Abstracts.pdf

Oral Transmissibility of Prion Disease Is Enhanced by Binding to Soil Particles

Christopher J. Johnson1,2, Joel A. Pedersen3, Rick J. Chappell4, Debbie McKenzie2, Judd M. Aiken1,2*

1 Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America, 2 Department of Comparative Biosciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America, 3 Department of Soil Science and Molecular and Environmental Toxicology Center, University of Wisconsin-Madison, Madison, Wisconsin, United States of America, 4 Biostatistics and Medical Informatics, University of Wisconsin Medical School, Madison, Wisconsin, United States of America

Soil may serve as an environmental reservoir for prion infectivity and contribute to the horizontal transmission of prion diseases (transmissible spongiform encephalopathies [TSEs]) of sheep, deer, and elk. TSE infectivity can persist in soil for years, and we previously demonstrated that the disease-associated form of the prion protein binds to soil particles and prions adsorbed to the common soil mineral montmorillonite (Mte) retain infectivity following intracerebral inoculation. Here, we assess the oral infectivity of Mte- and soil-bound prions. We establish that prions bound to Mte are orally bioavailable, and that, unexpectedly, binding to Mte significantly enhances disease penetrance and reduces the incubation period relative to unbound agent. Cox proportional hazards modeling revealed that across the doses of TSE agent tested, Mte increased the effective infectious titer by a factor of 680 relative to unbound agent. Oral exposure to Mte-associated prions led to TSE development in experimental animals even at doses too low to produce clinical symptoms in the absence of the mineral. We tested the oral infectivity of prions bound to three whole soils differing in texture, mineralogy, and organic carbon content and found soil- bound prions to be orally infectious. Two of the three soils increased oral transmission of disease, and the infectivity of agent bound to the third organic carbon-rich soil was equivalent to that of unbound agent. Enhanced transmissibility of soil-bound prions may explain the environmental spread of some TSEs despite the presumably low levels shed into the environment. Association of prions with inorganic microparticles represents a novel means by which their oral transmission is enhanced relative to unbound agent.

snip...

Discussion These experiments address the critical question of whether soil particle­bound prions are infectious by an environmentally relevant exposure route, namely, oral ingestion. Oral infectivity of soil particle­bound prions is a conditio sine qua non for soil to serve as an environmental reservoir for TSE agent. The maintenance of infectivity and enhanced transmissibility when TSE agent is bound to the common soil mineral Mte is remarkable given the avidity of the PrPTSE­Mte interaction [22]. One might expect the avid interaction of PrPTSE with Mte to result in the mineral serving as a sink, rather than a reservoir, for TSE infectivity. Our results demonstrate this may not be the case. Furthermore, sorption of prions to complex whole soils did not diminish bioavailability, and in two of three cases promoted disease transmission by the oral route of exposure. While extrapolation of these results to environmental conditions must be made with care, prion sorption to soil particles clearly has the potential to increase disease transmission via the oral route and contribute to the maintenance of TSE epizootics.

Two of three tested soils potentiated oral prion disease transmission. The reason for increased oral transmissibility associated with some, but not all, of the soils remains to be elucidated. One possibility is that components responsible for enhancing oral transmissibility were present at higher levels in the Elliot and Bluestem soils than in the Dodge soil. The major difference between the Dodge soil and the other two soils was the extremely high natural organic matter content of the former (34%, [22]). The Dodge and Elliot soils contained similar levels of mixed-layer illite/smectite, although the contribution of smectite layers was higher in the Dodge soil (14%­16%, [22]). The organic matter present in the Dodge soil may have obstructed access of PrPTSE to sorption sites on smectite (or other mineral) surfaces.

The mechanism by which Mte or other soil components enhances the oral transmissibility of particle-bound prions remains to be clarified. Aluminosilicate minerals such as Mte do not provoke inflammation of the intestinal lining [39]. Although such an effect is conceivable for whole soils, soil ingestion is common in ruminants and other mammals [25]. Prion binding to Mte or other soil components may partially protect PrPTSE from denaturation or proteolysis in the digestive tract [22,40] allowing more disease agent to be taken up from the gut than would otherwise be the case. Adsorption of PrPTSE to soil or soil minerals may alter the aggregation state of the protein, shifting the size distribution toward more infectious prion protein particles, thereby increasing the specific titer (i.e., infectious units per mass of protein) [41]. In the intestine, PrPTSE complexed with soil particles may be more readily sampled, endocytosed (e.g., at Peyer's patches), or persorbed than unbound prions. Aluminosilicate (as well as titanium dioxide, starch, and silica) microparticles, similar in size to the Mte used in our experiments, readily undergo endocytotic and persorptive uptake in the small intestine [42­44]. Enhanced translocation of the infectious agent from the gut lumen into the body may be responsible for the observed increase in transmission efficiency.

Survival analysis indicated that when bound to Mte, prions from both BH and purified PrPTSE preparations were more orally infectious than unbound agent. Mte addition influenced the effective titer of infected BH to a lesser extent than purified PrPTSE. Several nonmutually exclusive factors may explain this result: (1) other macromolecules present in BH (e.g., lipids, nucleic acids, other proteins) compete with PrPTSE for Mte binding sites; (2) prion protein is more aggregated in the purified PrPTSE preparation than in BH [45], and sorption to Mte reduces PrPTSE aggregate size, increasing specific titer [41]; and (3) sorption of macromolecules present in BH to Mte influences mineral particle uptake in the gut by altering surface charge or size, whereas the approximately 1,000-fold lower total protein concentration in purified PrPTSE preparations did not produce this effect.

We previously showed that other inorganic microparticles (kaolinite and silicon dioxide) also bind PrPTSE [22]. All three types of microparticles are widely used food additives and are typically listed as bentonite (Mte), kaolin (kaolinite), and silica (silicon dioxide). Microparticles are increasingly included in Western diets. Dietary microparticles are typically inert and considered safe for consumption by themselves, do not cause inflammatory responses or other pathologies, even with chronic consumption, and are often sampled in the gut and transferred from the intestinal lumen to lymphoid tissue [39,46,47]. Our data suggest that the binding of PrPTSE to dietary microparticles has the potential to enhance oral prion disease transmission and warrants further investigation.

In conclusion, our results provide compelling support for the hypothesis that soil serves as a biologically relevant reservoir of TSE infectivity. Our data are intriguing in light of reports that naïve animals can contract TSEs following exposure to presumably low doses of agent in the environment [5,7­9]. We find that Mte enhances the likelihood of TSE manifestation in cases that would otherwise remain subclinical (Figure 3B and 3C), and that prions bound to soil are orally infectious (Figure 5). Our results demonstrate that adsorption of TSE agent to inorganic microparticles and certain soils alter transmission efficiency via the oral route of exposure.

snip...

full text is here:

http://pathogens.plosjournals.org/perlserv/?request=get-document&doi=10....

http://pathogens.plosjournals.org/perlserv/?request=get-pdf&file=10.1371...

http://pathogens.plosjournals.org/perlserv/?request=get-pdf&file=10.1371...

From: TSS (216-119-163-189.ipset45.wt.net)
Subject: CWD aka MAD DEER/ELK TO HUMANS ???
Date: September 30, 2002 at 7:06 am PST

From: "Belay, Ermias"
To:
Cc: "Race, Richard (NIH)" ; ; "Belay,
Ermias"
Sent: Monday, September 30, 2002 9:22 AM
Subject: RE: TO CDC AND NIH - PUB MED- 3 MORE DEATHS - CWD - YOUNG HUNTERS

> Dear Sir/Madam,
> In the Archives of Neurology you quoted (the abstract of which was

attached

> to your email), we did not say CWD in humans will present like variant

CJD.

> That assumption would be wrong. I encourage you to read the whole
article
> and call me if you have questions or need more clarification (phone:
> 404-639-3091). Also, we do not claim that "no-one has ever been
infected
> with prion disease from eating venison." Our conclusion stating that we
> found no strong evidence of CWD transmission to humans in the
article you
> quoted or in any other forum is limited to the patients we
investigated.
>
> Ermias Belay, M.D.
> Centers for Disease Control and Prevention
>

> > -----Original Message-----
> > From:
> > Sent: Sunday, September 29, 2002 10:15 AM
> > To: rr26k@nih.gov; rrace@niaid.nih.gov; ebb8@CDC.GOV
> > Subject: TO CDC AND NIH - PUB MED- 3 MORE DEATHS - CWD - YOUNG
> > HUNTERS

Aguzzi warns of CWD danger

The TSE family of diseases also includes chronic wasting disease (CWD)
in deer, a condition that has spread in the US in recent years (Nature
416, 569; 2002). Speaking at the Days of Molecular Medicine conference
in La Jolla in March, prion expert Adriano Aguzzi issued a strong
warning against underestimating this form of TSE.

"For more than a decade, the US has by-and-large considered mad cows
to be an exquisitely European problem. The perceived need to protect
US citizens from this alien threat has even prompted the deferral of
blood donors from Europe," he said. "Yet the threat-from-within
posed by CWD needs careful consideration, since the evidence that CWD
is less dangerous to humans than BSE is less-than-complete. Aguzzi
went on to point out that CWD is arguably the most mysterious of all
prion diseases.

"Its horizontal spread among the wild population is exceedingly
efficient, and appears to have reached a prevalence unprecedented even
by BSE in the UK at its peak. The pathogenesis of CWD, therefore,
deserves a vigorous research effort. Europeans also need to think
about this problem, and it would be timely and appropriate to increase
CWD surveillance in Europe too." Aguzzi has secured funding from the
National Institutes of Health to investigate CWD, and the effort will
be lead by Christina Sigurdson in his department at the University of
Zurich. KAREN BIRMINGHAM, LONDON

This quote from Dr. Gambetti is especially significant since he is the
rather cautious TSE researcher under contract with the Centers for Disease
Control to examine the brains of individuals who have died of CJD.
-----------------

Pierluigi Gambetti, director of the National Prion Disease Pathology
Surveillance Center at Case Western Reserve University in Cleveland,
said all deer should be tested for chronic wasting disease before any
processing is done.

"There is no way around it," he said. "Nobody should touch that meat
unless it has been tested."
--------------------------------------

http://www.ledger-enquirer.com/mld/...ion/3954298.htm
================================================== ====

'As implied in the Inset 25 we must not assume that transmission
of BSE to other species will invariably present pathology typical
of a scrapie-like disease.'

http://www.bse.org.uk/files/yb/1991/01/04004001.pdf

see full text ;

Re: Colorado Surveillance Program for Chronic Wasting Disease
Transmission to Humans (TWO SUSPECT CASES)

http://lists.ifas.ufl.edu/cgi-bin/wa.exe?A2=ind0704&L=sanet-mg&T=0&P=1165

doi:10.1016/S1473-3099(03)00715-1
Copyright © 2003 Published by Elsevier Ltd.
Newsdesk

Tracking spongiform encephalopathies in North America

Xavier Bosch

Available online 29 July 2003.

Volume 3, Issue 8, August 2003, Page 463

“My name is Terry S Singeltary Sr, and I live in Bacliff, Texas. I lost my
mom to hvCJD (Heidenhain variant CJD)
and have been searching for answers ever since. What I have found is that we
have not been told the truth. CWD
in deer and elk is a small portion of a much bigger problem.”
............................

http://www.thelancet.com/journals/laninf/article/PIIS1473309903007151/fu...

http://download.thelancet.com/pdfs/journals/1473-3099/PIIS14733099030071...

TSS