Louisiana business, 3 men accused of smuggling deer into Mississippi
Update: Louisiana business, 3 men accused of smuggling deer into
Mississippi
Trial set for March 17 in Gulfport
By ROBIN FITZGERALD
February 12, 2014
GULFPORT -- A federal grand jury has indicted a Louisiana business and
three associates on charges alleging they conspired to import white-tailed deer
from other states into wildlife enclosures in Pearl River and Lamar counties for
the breeding and killing of trophy bucks.
Omni Pinnacle LLC, Brian R. Reine, Ronald W. Reine and Bruce A. Swilley Jr.
are set for trial March 17 in U.S. District Court in Gulfport. They were
arraigned Wednesday and were released on unsecured bonds of $25,000 each.
State and federal laws prohibit importing white-tailed deer into
Mississippi to protect the deer population from chronic wasting disease and
bovine tuberculosis.
The company and the men are accused of violating the federal Lacey Act,
which mirrors a state law aimed at preventing infectious diseases among
white-tailed deer.
Omni Pinnacle is a disaster debris-management company based in Pearl River,
La. Brian Reine, 44, is its chief executive officer and director of operations,
according to the company web site. Ronald Reine, 67, is a consultant and
assistant project manager. Swilley, 27, is not listed as an employee on the web
site.
The three men are accused of conspiring to smuggle deer onto wildlife
enclosures managed by the Reines in Mississippi from January 2011 through
December 2012. Deer placed at the wildlife enclosures also were used for deer
hunts for business development and public relations for Omni Pinnacle, the
indictment says.
The government alleges the men imported deer from Kentucky, Indiana,
Pennsylvania and Louisiana to Hunter's Bluff, also known as Oak Investments LLC,
a wildlife enclosure under Ronald Reine's control in Pearl River County and Half
Moon Ranch, operated in Lamar County by Brian Reine.
Swilley went to the different states to handle the shipments, the
indictment said.
Swilley and Brian Reine also are accused of making false statements to the
sellers or on Certificates of Veterinary Inspection by claiming the deer were
being taken to Louisiana, not Mississippi.
"The importation of white-tailed deer into Mississippi is a growing problem
with the potential for a devastating impact on our native deer herd," U.S.
Attorney Gregory K. Davis said in a news release.
Chronic wasting disease spreads easily among mammals and can decimate
native herds. CWD has been found in 18 states as of November, according to the
Centers for Disease and Poison Control. Some states have killed tens of
thousands of deer to get rid of the disease.
Bovine tuberculosis is a contagious bacterial disease that can spread to
other animals and humans.
The CDC recommends not eating diseased deer or under-cooked deer
meat.
The 13-count indictment includes a forfeiture notice that the government
plans to seize all deer brought into Mississippi, a 2009 Ford truck and a
breeding trailer.
The indictment does not identify the number of deer.
If convicted, the company faces a maximum fine of $500,000. The men each
face up to five years in prison and a $250,000 fine for each count.
The company and all three were indicted on a conspiracy charge. Brian Reine
faces 12 counts of related violations. Swilley faces eight additional counts.
Ronald Reine faces one additional count.
The case was investigated by the U.S. Fish and Wildlife Service and the
Mississippi Department of Wildlife, Fisheries and Parks.
The prosecutor is Assistant U.S. Attorney Darren J. LaMarca.
The white-tailed deer was named the state's official mammal in 1974.
NICE BUST ! whomever is responsible...
nothing like spreading it all around though $$$ and CWD
Wisconsin tracks 81 deer from game farm with CWD buck to seven other states
State tracks 81 deer from game farm with CWD buck
By Lee Bergquist of the Journal Sentinel Feb. 11, 2014 5:18 p.m.
The state agriculture department said Tuesday that 81 deer have been traced
to farms in Wisconsin and seven other states from a deer operation that produced
the first case of chronic wasting disease at a game farm in five years.
The Department of Agriculture, Trade and Consumer Protection said Dec. 2
that a male deer from a shooting preserve in Marathon County that was killed on
Nov. 4 had tested positive for the fatal deer disease.
The owners of the shooting preserve, Wilderness Whitetails, also own
breeding farms in Portage County, where the male was kept from May 2008 to
September 2010, according to the agriculture department.
Paul McGraw, the state veterinarian, said his agency found through records
that the male deer lived at the same breeding farm as the other deer that have
since been moved to other facilities, although an owner of the farm said there
was no contact between the male deer and the deer.
Eight were traced to Antler Valley Whitetails in Kaukauna in Outagamie
County and five were traced to Clam River Whitetails of Webster in Burnett
County, McGraw said.
Also, 68 deer were shipped to game farms in Minnesota, Illinois, Ohio,
Pennsylvania, Missouri, Oklahoma and Louisiana.
snip...
Tuesday, February 11, 2014
Wisconsin tracks 81 deer from game farm with CWD buck to seven other states
Thursday, October 03, 2013
TAHC ADOPTS CWD RULE THAT the amendments REMOVE the requirement for a
specific fence height for captives
Texas Animal Health Commission (TAHC) ANNOUNCEMENT October 3, 2013
Tuesday, February 04, 2014
Indiana Hunting preserves Sen. Carlin Yoder Senate Bill 404 and Rep.
William Friend House Bill 1154 DEAD IN THE WATER ?
Saturday, June 29, 2013
PENNSYLVANIA CAPTIVE CWD INDEX HERD MATE YELLOW *47 STILL RUNNING LOOSE IN
INDIANA, YELLOW NUMBER 2 STILL MISSING, AND OTHERS ON THE RUN STILL IN LOUISIANA
Monday, June 24, 2013
The Effects of Chronic Wasting Disease on the Pennsylvania Cervid Industry
Following its Discovery
Tuesday, June 11, 2013
CWD GONE WILD, More cervid escapees from more shooting pens on the loose in
Pennsylvania
Tuesday, May 28, 2013
Chronic Wasting Disease CWD quarantine Louisiana via CWD index herd
Pennsylvania Update May 28, 2013
6 doe from Pennsylvania CWD index herd still on the loose in Louisiana,
quarantine began on October 18, 2012, still ongoing, Lake Charles premises.
Wednesday, August 21, 2013
IOWA DNR EMERGENCY CONSENT ORDER IN THE MATTER OF TOM & LINDA BRAKKE
D/B/A PINE RIDGE HUNTING LODGE UPDATE AUGUST 21, 2013
snip...
5. On July 16, 2012, DNR received a notice from the Texas Veterinary
Medical Diagnostic Lab ("Texas Vet Lab”) that a sample from an adult male deer
killed at Pine Ridge tested presumptively positive for CWD. (DNR has an
agreement with the Texas Vet Lab to run these preliminary tests.) Because the
Texas Vet Lab found this presumptive positive result, protocols required the
sample to be sent to the National Veterinary Services Laboratory ("National
Lab”) in Ames, Iowa for final confirmation. On July 18, 2012, the National Lab
confirmed the positive CWD result in the deer.
6. On July 19, 2012, DNR notified the Brakkes of the positive test by
phone. Mr. Brakke was out of state.
snip...
12. The Brakkes depopulated the Hunting Preserve, as specified in the
Agreement, from September 10, 2012 to January 31, 2013. As part of this effort,
the Brakkes, the staff and their customers killed 199 captive deer and nine
captive elk. The DNR obtained 170 CWD samples. (Samples were not taken from
fawns and one adult female who was killed in a manner that made sampling
impossible.) Of these 199 deer, two additional adult male deer tested positive
for CWD. Information provided by the Brakkes confirmed that these two additional
deer originated from the Brakke Breeding Facility.
13. DNR installed, with the Brakke's permission, an interior electric fence
on October 1 and 2, 2012.
14. The Brakkes cleaned and disinfected, under DNR supervision, the feeders
and ground surrounding the feeders on April 5, 2013.
15. On April 26, 2013, the Brakkes hand-delivered a notice to the DNR’s
Chief of Law Enforcement Bureau, notifying the DNR that they would no longer
operate a hunting preserve on the Quarantined Premises. The Brakkes did not
reveal any plans to remove the fence around the Quarantined Premises or to
remove the gates to and from the Quarantined Premises in this April 26, 2013
letter.
16. On June 3, 2013, DNR became aware that sections of the exterior fence
surrounding the Quarantined Premises had been removed and that some, if not all,
of the exterior gates to and from the Quarantined Premises were open.
17. On June 4, 2013, DNR received reports from the public in the area that
four wild deer were observed inside the Quarantined Premises.
18. On June 5, 2013, DNR conducted a fence inspection, after gaining
approval from surrounding landowners, and confirmed that the fenced had been cut
or removed in at least four separate locations; that the fence had degraded and
was failing to maintain the enclosure around the Quarantined Premises in at
least one area; that at least three gates had been opened; and that deer tracks
were visible in and around one of the open areas in the sand on both sides of
the fence, evidencing movement of deer into the Quarantined Premises.
IV. CONCLUSIONS OF LAW
snip...
Wednesday, August 21, 2013
IOWA DNR EMERGENCY CONSENT ORDER IN THE MATTER OF TOM & LINDA BRAKKE
D/B/A PINE RIDGE HUNTING LODGE UPDATE AUGUST 21, 2013
Wednesday, September 04, 2013
*** cwd - cervid captive livestock escapes, loose and on the run in the
wild
pens, pens, PENS ???
*** Spraker suggested an interesting explanation for the occurrence of CWD.
The deer pens at the Foot Hills Campus were built some 30-40 years ago by a Dr.
Bob Davis. At or abut that time, allegedly, some scrapie work was conducted at
this site. When deer were introduced to the pens they occupied ground that had
previously been occupied by sheep. ...
also, see where even decades back, the USDA had the same thought as they do
today with CWD, not their problem...see page 27 below as well, where USDA stated
back then, the same thing they stated in the state of Pennsylvania, not their
damn business, once they escape, and they said the same thing about CWD in
general back then ;
”The occurrence of CWD must be viewed against the contest of the locations
in which it occurred. It was an incidental and unwelcome complication of the
respective wildlife research programmes. Despite it’s subsequent recognition as
a new disease of cervids, therefore justifying direct investigation, no specific
research funding was forthcoming. The USDA veiwed it as a wildlife problem and
consequently not their province!” ...page 26.
”The occurrence of CWD must be viewed against the contest of the locations
in which it occurred. It was an incidental and unwelcome complication of the
respective wildlife research programmes. Despite it’s subsequent recognition as
a new disease of cervids, therefore justifying direct investigation, no specific
research funding was forthcoming. The USDA veiwed it as a wildlife problem and
consequently not their province!” ...page 26.
sound familiar $$$
Sunday, January 06, 2013
USDA TO PGC ONCE CAPTIVES ESCAPE
*** "it‘s no longer its business.”
*** PRICE OF CWD TSE PRION POKER GOES UP 2014 ***
Transmissible Spongiform Encephalopathy TSE PRION update January 2, 2014
*** chronic wasting disease, there was no absolute barrier to conversion of
the human prion protein.
*** Furthermore, the form of human PrPres produced in this in vitro assay
when seeded with CWD, resembles that found in the most common human prion
disease, namely sCJD of the MM1 subtype.
*** The potential impact of prion diseases on human health was greatly
magnified by the recognition that interspecies transfer of BSE to humans by beef
ingestion resulted in vCJD. While changes in animal feed constituents and
slaughter practices appear to have curtailed vCJD, there is concern that CWD of
free-ranging deer and elk in the U.S. might also cross the species barrier.
Thus, consuming venison could be a source of human prion disease. Whether BSE
and CWD represent interspecies scrapie transfer or are newly arisen prion
diseases is unknown. Therefore, the possibility of transmission of prion disease
through other food animals cannot be ruled out. There is evidence that vCJD can
be transmitted through blood transfusion. There is likely a pool of unknown size
of asymptomatic individuals infected with vCJD, and there may be asymptomatic
individuals infected with the CWD equivalent. These circumstances represent a
potential threat to blood, blood products, and plasma supplies.
Thursday, January 2, 2014
*** CWD TSE Prion in cervids to hTGmice, Heidenhain Variant
Creutzfeldt-Jacob Disease MM1 genotype, and iatrogenic CJD ??? ***
Wednesday, January 01, 2014
APHIS-2006-0118-0100 Chronic Wasting Disease Herd Certification Program and
Interstate Movement of Farmed or Captive Deer, Elk, and Moose
The chances of a person or domestic animal contracting CWD are “extremely
remote,” Richards said. The possibility can’t be ruled out, however. “One could
look at it like a game of chance,” he explained. “The odds (of infection)
increase over time because of repeated exposure. That’s one of the downsides of
having CWD in free-ranging herds: We’ve got this infectious agent out there that
we can never say never to in terms of (infecting) people and domestic
livestock.”
P35
ADAPTATION OF CHRONIC WASTING DISEASE (CWD) INTO HAMSTERS, EVIDENCE OF A
WISCONSIN STRAIN OF CWD
Chad Johnson1, Judd Aiken2,3,4 and Debbie McKenzie4,5 1 Department of
Comparative Biosciences, University of Wisconsin, Madison WI, USA 53706 2
Department of Agriculture, Food and Nutritional Sciences, 3 Alberta Veterinary
Research Institute, 4.Center for Prions and Protein Folding Diseases, 5
Department of Biological Sciences, University of Alberta, Edmonton AB, Canada
T6G 2P5
The identification and characterization of prion strains is increasingly
important for the diagnosis and biological definition of these infectious
pathogens. Although well-established in scrapie and, more recently, in BSE,
comparatively little is known about the possibility of prion strains in chronic
wasting disease (CWD), a disease affecting free ranging and captive cervids,
primarily in North America. We have identified prion protein variants in the
white-tailed deer population and demonstrated that Prnp genotype affects the
susceptibility/disease progression of white-tailed deer to CWD agent. The
existence of cervid prion protein variants raises the likelihood of distinct CWD
strains. Small rodent models are a useful means of identifying prion strains. We
intracerebrally inoculated hamsters with brain homogenates and phosphotungstate
concentrated preparations from CWD positive hunter-harvested (Wisconsin CWD
endemic area) and experimentally infected deer of known Prnp genotypes. These
transmission studies resulted in clinical presentation in primary passage of
concentrated CWD prions. Subclinical infection was established with the other
primary passages based on the detection of PrPCWD in the brains of hamsters and
the successful disease transmission upon second passage. Second and third
passage data, when compared to transmission studies using different CWD inocula
(Raymond et al., 2007) indicate that the CWD agent present in the Wisconsin
white-tailed deer population is different than the strain(s) present in elk,
mule-deer and white-tailed deer from the western United States endemic region.
PPo3-7:
Prion Transmission from Cervids to Humans is Strain-dependent
Qingzhong Kong, Shenghai Huang,*Fusong Chen, Michael Payne, Pierluigi
Gambetti and Liuting Qing Department of Pathology; Case western Reserve
University; Cleveland, OH USA *Current address: Nursing Informatics; Memorial
Sloan-Kettering Cancer Center; New York, NY USA
Key words: CWD, strain, human transmission
Chronic wasting disease (CWD) is a widespread prion disease in cervids
(deer and elk) in North America where significant human exposure to CWD is
likely and zoonotic transmission of CWD is a concern. Current evidence indicates
a strong barrier for transmission of the classical CWD strain to humans with the
PrP-129MM genotype. A few recent reports suggest the presence of two or more CWD
strains. What remain unknown is whether individuals with the PrP-129VV/MV
genotypes are also resistant to the classical CWD strain and whether humans are
resistant to all natural or adapted cervid prion strains. Here we report that a
human prion strain that had adopted the cervid prion protein (PrP) sequence
through passage in cervidized transgenic mice efficiently infected transgenic
mice expressing human PrP, indicating that the species barrier from cervid to
humans is prion strain-dependent and humans can be vulnerable to novel cervid
prion strains. Preliminary results on CWD transmission in transgenic mice
expressing human PrP-129V will also be discussed.
Acknowledgement Supported by NINDS NS052319 and NIA AG14359.
PPo2-27:
Generation of a Novel form of Human PrPSc by Inter-species Transmission of
Cervid Prions
Marcelo A. Barria,1 Glenn C. Telling,2 Pierluigi Gambetti,3 James A.
Mastrianni4 and Claudio Soto1 1Mitchell Center for Alzheimer's disease and
related Brain disorders; Dept of Neurology; University of Texas Houston Medical
School; Houston, TX USA; 2Dept of Microbiology, Immunology & Molecular
Genetics and Neurology; Sanders Brown Center on Aging; University of Kentucky
Medical Center; Lexington, KY USA; 3Institute of Pathology; Case western Reserve
University; Cleveland, OH USA; 4Dept of Neurology; University of Chicago;
Chicago, IL USA
Prion diseases are infectious neurodegenerative disorders affecting humans
and animals that result from the conversion of normal prion protein (PrPC) into
the misfolded and infectious prion (PrPSc). Chronic wasting disease (CWD) of
cervids is a prion disorder of increasing prevalence within the United States
that affects a large population of wild and captive deer and elk. CWD is highly
contagious and its origin, mechanism of transmission and exact prevalence are
currently unclear. The risk of transmission of CWD to humans is unknown.
Defining that risk is of utmost importance, considering that people have been
infected by animal prions, resulting in new fatal diseases. To study the
possibility that human PrPC can be converted into the infectious form by CWD
PrPSc we performed experiments using the Protein Misfolding Cyclic Amplification
(PMCA) technique, which mimic in vitro the process of prion replication. Our
results show that cervid PrPSc can induce the pathological conversion of human
PrPC, but only after the CWD prion strain has been stabilized by successive
passages in vitro or in vivo. Interestingly, this newly generated human PrPSc
exhibits a distinct biochemical pattern that differs from any of the currently
known forms of human PrPSc, indicating that it corresponds to a novel human
prion strain. Our findings suggest that CWD prions have the capability to infect
humans, and that this ability depends on CWD strain adaptation, implying that
the risk for human health progressively increases with the spread of CWD among
cervids.
PPo2-7:
Biochemical and Biophysical Characterization of Different CWD
Isolates
Martin L. Daus and Michael Beekes Robert Koch Institute; Berlin,
Germany
Key words: CWD, strains, FT-IR, AFM
Chronic wasting disease (CWD) is one of three naturally occurring forms of
prion disease. The other two are Creutzfeldt-Jakob disease in humans and scrapie
in sheep. CWD is contagious and affects captive as well as free ranging cervids.
As long as there is no definite answer of whether CWD can breach the species
barrier to humans precautionary measures especially for the protection of
consumers need to be considered. In principle, different strains of CWD may be
associated with different risks of transmission to humans. Sophisticated strain
differentiation as accomplished for other prion diseases has not yet been
established for CWD. However, several different findings indicate that there
exists more than one strain of CWD agent in cervids. We have analysed a set of
CWD isolates from white-tailed deer and could detect at least two biochemically
different forms of disease-associated prion protein PrPTSE. Limited proteolysis
with different concentrations of proteinase K and/or after exposure of PrPTSE to
different pH-values or concentrations of Guanidinium hydrochloride resulted in
distinct isolate-specific digestion patterns. Our CWD isolates were also
examined in protein misfolding cyclic amplification studies. This showed
different conversion activities for those isolates that had displayed
significantly different sensitivities to limited proteolysis by PK in the
biochemical experiments described above. We further applied Fourier transform
infrared spectroscopy in combination with atomic force microscopy. This
confirmed structural differences in the PrPTSE of at least two disinct CWD
isolates. The data presented here substantiate and expand previous reports on
the existence of different CWD strains.
2012
Envt.06:
Zoonotic Potential of CWD: Experimental Transmissions to Non-Human Primates
Emmanuel Comoy,1,† Valérie Durand,1 Evelyne Correia,1 Aru Balachandran,2
Jürgen Richt,3 Vincent Beringue,4 Juan-Maria Torres,5 Paul Brown,1 Bob Hills6
and Jean-Philippe Deslys1
1Atomic Energy Commission; Fontenay-aux-Roses, France; 2Canadian Food
Inspection Agency; Ottawa, ON Canada; 3Kansas State University; Manhattan, KS
USA; 4INRA; Jouy-en-Josas, France; 5INIA; Madrid, Spain; 6Health Canada; Ottawa,
ON Canada
†Presenting author; Email: emmanuel.comoy@cea.fr
The constant increase of chronic wasting disease (CWD) incidence in North
America raises a question about their zoonotic potential. A recent publication
showed their transmissibility to new-world monkeys, but no transmission to
old-world monkeys, which are phylogenetically closer to humans, has so far been
reported. Moreover, several studies have failed to transmit CWD to transgenic
mice overexpressing human PrP. Bovine spongiform encephalopathy (BSE) is the
only animal prion disease for which a zoonotic potential has been proven. We
described the transmission of the atypical BSE-L strain of BSE to cynomolgus
monkeys, suggesting a weak cattle-to-primate species barrier. We observed the
same phenomenon with a cattleadapted strain of TME (Transmissible Mink
Encephalopathy). Since cattle experimentally exposed to CWD strains have also
developed spongiform encephalopathies, we inoculated brain tissue from
CWD-infected cattle to three cynomolgus macaques as well as to transgenic mice
overexpressing bovine or human PrP. Since CWD prion strains are highly
lymphotropic, suggesting an adaptation of these agents after peripheral
exposure, a parallel set of four monkeys was inoculated with CWD-infected cervid
brains using the oral route. Nearly four years post-exposure, monkeys exposed to
CWD-related prion strains remain asymptomatic. In contrast, bovinized and
humanized transgenic mice showed signs of infection, suggesting that CWD-related
prion strains may be capable of crossing the cattle-to-primate species barrier.
Comparisons with transmission results and incubation periods obtained after
exposure to other cattle prion strains (c-BSE, BSE-L, BSE-H and cattle-adapted
TME) will also be presented, in order to evaluate the respective risks of each
strain.
Envt.07:
Pathological Prion Protein (PrPTSE) in Skeletal Muscles of Farmed and Free
Ranging White-Tailed Deer Infected with Chronic Wasting Disease
Martin L. Daus,1,† Johanna Breyer,2 Katjs Wagenfuehr,1 Wiebke Wemheuer,2
Achim Thomzig,1 Walter Schulz-Schaeffer2 and Michael Beekes1 1Robert Koch
Institut; P24 TSE; Berlin, Germany; 2Department of Neuropathology, Prion and
Dementia Research Unit, University Medical Center Göttingen; Göttingen, Germany
†Presenting author; Email: dausm@rki.de
Chronic wasting disease (CWD) is a contagious, rapidly spreading
transmissible spongiform encephalopathy (TSE) occurring in cervids 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 a direct biochemical demonstration of pathological prion protein PrPTSE
and of PrPTSE-associated seeding activity in skeletal muscles of CWD-infected
cervids. 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). The concentration of PrPTSE in skeletal
muscles of CWD-infected WTD was estimated to be approximately 2000- to
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.
Sunday, August 19, 2012
Susceptibility of cattle to the agent of chronic wasting disease from elk
after intracranial inoculation 2012
Research Project: TRANSMISSION, DIFFERENTIATION, AND PATHOBIOLOGY OF
TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES Location: Virus and Prion Research
Unit
PO-081: Chronic wasting disease in the cat— Similarities to feline
spongiform encephalopathy (FSE)
PO-081: Chronic wasting disease in the cat— Similarities to feline
spongiform encephalopathy (FSE)
PRION2013 CONGRESSIONAL ABSTRACTS CWD
Sunday, August 25, 2013
HD.13: CWD infection in the spleen of humanized
transgenic mice
Liuting Qing and Qingzhong Kong
Case Western Reserve University; Cleveland, OH
USA
Chronic wasting disease (CWD) is a widespread
prion disease in free-ranging and captive cervid species in North America, and
there is evidence suggesting the existence of multiple CWD strains. The
susceptibility of human CNS and peripheral organs to the various CWD prion
strains remains largely unclear. Current literature suggests that the classical
CWD strain is unlikely to infect human brain, but the potential for peripheral
infection by CWD in humans is unknown. We detected protease-resistant PrpSc in
the spleens of a few humanized transgenic mice that were intracerebrally
inoculated with natural CWD isolates, but PrpSc was not detected in the brains
of any of the CWD-inoculated mice. Our ongoing bioassays in humanized Tg mice
indicate that intracerebral challenge with such PrpSc-positive humanized mouse
spleen already led to prion disease in most animals. ***These results indicate
that the CWD prion may have the potential to infect human peripheral lymphoid
tissues.
Oral.15: Molecular barriers to zoonotic prion
transmission: Comparison of the ability of sheep, cattle and deer prion disease
isolates to convert normal human prion protein to its pathological isoform in a
cell-free system
Marcelo A.Barria,1 Aru Balachandran,2 Masanori
Morita,3 Tetsuyuki Kitamoto,4 Rona Barron,5 Jean Manson,5 Richard Kniqht,1 James
W. lronside1 and Mark W. Head1
1National CJD Research and Surveillance Unit;
Centre for Clinical Brain Sciences; School of Clinical Sciences; The University
of Edinburgh; Edinburgh, UK; 2National and OIE Reference Laboratory for Scrapie
and CWD; Canadian Food Inspection Agency; Ottawa Laboratory; Fallowfield. ON
Canada; 3Infectious Pathogen Research Section; Central Research Laboratory;
Japan Blood Products Organization; Kobe, Japan; 4Department of Neurological
Science; Tohoku University Graduate School of Medicine; Sendai. Japan;
5Neurobiology Division; The Roslin Institute and R(D)SVS; University of
Edinburgh; Easter Bush; Midlothian; Edinburgh, UK
Background. Bovine spongiform encephalopathy
(BSE) is a known zoonotic prion disease, resulting in variant Creurzfeldt- Jakob
disease (vCJD) in humans. In contrast, classical scrapie in sheep is thought to
offer little or no danger to human health. However, a widening range of prion
diseases have been recognized in cattle, sheep and deer. The risks posed by
individual animal prion diseases to human health cannot be determined a priori
and are difficult to assess empirically. The fundamemal event in prion disease
pathogenesis is thought to be the seeded conversion of normal prion protein
(PrPC) to its pathological isoform (PrPSc). Here we report the use of a rapid
molecular conversion assay to test whether brain specimens from different animal
prion diseases are capable of seeding the conversion of human PrPC ro PrPSc.
Material and Methods. Classical BSE (C-type BSE),
H-type BSE, L-type BSE, classical scrapie, atypical scrapie, chronic wasting
disease and vCJD brain homogenates were tested for their ability to seed
conversion of human PrPC to PrPSc in protein misfolding cyclic amplification
(PMCA) reactions. Newly formed human PrPSc was detected by protease digestion
and western blotting using the antibody 3F4.
Results. C-type BSE and vCJD were found to
efficiently convert PrPC to PrPSc. Scrapie failed to convert human PrPC to
PrPSc. Of the other animal prion diseases tested only chronic wasting disease
appeared to have the capability ro convert human PrPC to PrPSc. The results were
consistent whether the human PrPC came from human brain, humanised transgenic
mouse brain or from cultured human cells and the effect was more pronounced for
PrPC with methionine at codon 129 compared with that with valine.
Conclusion. Our results show that none of the
tested animal prion disease isolates are as efficient as C-type BSE and vCJD in
converting human prion protein in this in vitro assay. ***However, they also
show that there is no absolute barrier ro conversion of human prion protein in
the case of chronic wasting disease.
PRION2013 CONGRESSIONAL ABSTRACTS CWD
Sunday, August 25, 2013
***Chronic Wasting Disease CWD risk factors,
humans, domestic cats, blood, and mother to offspring transmission
Sunday, July 21, 2013
*** As Chronic Wasting Disease CWD rises in deer
herd, what about risk for humans?
Envt.07:
Pathological Prion Protein (PrPTSE) in Skeletal
Muscles of Farmed and Free Ranging White-Tailed Deer Infected with Chronic
Wasting Disease
Martin L. Daus,1,† Johanna Breyer,2 Katjs
Wagenfuehr,1 Wiebke Wemheuer,2 Achim Thomzig,1 Walter Schulz-Schaeffer2 and
Michael Beekes1 1Robert Koch Institut; P24 TSE; Berlin, Germany; 2Department of
Neuropathology, Prion and Dementia Research Unit, University Medical Center
Göttingen; Göttingen, Germany †Presenting author; Email: dausm@rki.de
Chronic wasting disease (CWD) is a contagious,
rapidly spreading transmissible spongiform encephalopathy (TSE) occurring in
cervids 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 a direct biochemical demonstration of pathological
prion protein PrPTSE and of PrPTSE-associated seeding activity in skeletal
muscles of CWD-infected cervids. 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). The concentration of
PrPTSE in skeletal muscles of CWD-infected WTD was estimated to be approximately
2000- to 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.
PPo3-7:
Prion Transmission from Cervids to Humans is
Strain-dependent
Qingzhong Kong, Shenghai Huang,*Fusong Chen,
Michael Payne, Pierluigi Gambetti and Liuting Qing Department of Pathology; Case
western Reserve University; Cleveland, OH USA *Current address: Nursing
Informatics; Memorial Sloan-Kettering Cancer Center; New York, NY
USA
Key words: CWD, strain, human
transmission
Chronic wasting disease (CWD) is a widespread
prion disease in cervids (deer and elk) in North America where significant human
exposure to CWD is likely and zoonotic transmission of CWD is a concern. Current
evidence indicates a strong barrier for transmission of the classical CWD strain
to humans with the PrP-129MM genotype. A few recent reports suggest the presence
of two or more CWD strains. What remain unknown is whether individuals with the
PrP-129VV/MV genotypes are also resistant to the classical CWD strain and
whether humans are resistant to all natural or adapted cervid prion strains.
Here we report that a human prion strain that had adopted the cervid prion
protein (PrP) sequence through passage in cervidized transgenic mice efficiently
infected transgenic mice expressing human PrP, indicating that the species
barrier from cervid to humans is prion strain-dependent and humans can be
vulnerable to novel cervid prion strains. Preliminary results on CWD
transmission in transgenic mice expressing human PrP-129V will also be
discussed.
Acknowledgement Supported by NINDS NS052319 and
NIA AG14359.
PPo2-27:
Generation of a Novel form of Human PrPSc by
Inter-species Transmission of Cervid Prions
Marcelo A. Barria,1 Glenn C. Telling,2 Pierluigi
Gambetti,3 James A. Mastrianni4 and Claudio Soto1 1Mitchell Center for
Alzheimer's disease and related Brain disorders; Dept of Neurology; University
of Texas Houston Medical School; Houston, TX USA; 2Dept of Microbiology,
Immunology & Molecular Genetics and Neurology; Sanders Brown Center on
Aging; University of Kentucky Medical Center; Lexington, KY USA; 3Institute of
Pathology; Case western Reserve University; Cleveland, OH USA; 4Dept of
Neurology; University of Chicago; Chicago, IL USA
Prion diseases are infectious neurodegenerative
disorders affecting humans and animals that result from the conversion of normal
prion protein (PrPC) into the misfolded and infectious prion (PrPSc). Chronic
wasting disease (CWD) of cervids is a prion disorder of increasing prevalence
within the United States that affects a large population of wild and captive
deer and elk. CWD is highly contagious and its origin, mechanism of transmission
and exact prevalence are currently unclear. The risk of transmission of CWD to
humans is unknown. Defining that risk is of utmost importance, considering that
people have been infected by animal prions, resulting in new fatal diseases. To
study the possibility that human PrPC can be converted into the infectious form
by CWD PrPSc we performed experiments using the Protein Misfolding Cyclic
Amplification (PMCA) technique, which mimic in vitro the process of prion
replication. Our results show that cervid PrPSc can induce the pathological
conversion of human PrPC, but only after the CWD prion strain has been
stabilized by successive passages in vitro or in vivo. Interestingly, this newly
generated human PrPSc exhibits a distinct biochemical pattern that differs from
any of the currently known forms of human PrPSc, indicating that it corresponds
to a novel human prion strain. Our findings suggest that CWD prions have the
capability to infect humans, and that this ability depends on CWD strain
adaptation, implying that the risk for human health progressively increases with
the spread of CWD among cervids.
PPo2-7:
Biochemical and Biophysical Characterization of
Different CWD Isolates
Martin L. Daus and Michael Beekes Robert Koch
Institute; Berlin, Germany
Key words: CWD, strains, FT-IR,
AFM
Chronic wasting disease (CWD) is one of three
naturally occurring forms of prion disease. The other two are Creutzfeldt-Jakob
disease in humans and scrapie in sheep. CWD is contagious and affects captive as
well as free ranging cervids. As long as there is no definite answer of whether
CWD can breach the species barrier to humans precautionary measures especially
for the protection of consumers need to be considered. In principle, different
strains of CWD may be associated with different risks of transmission to humans.
Sophisticated strain differentiation as accomplished for other prion diseases
has not yet been established for CWD. However, several different findings
indicate that there exists more than one strain of CWD agent in cervids. We have
analysed a set of CWD isolates from white-tailed deer and could detect at least
two biochemically different forms of disease-associated prion protein PrPTSE.
Limited proteolysis with different concentrations of proteinase K and/or after
exposure of PrPTSE to different pH-values or concentrations of Guanidinium
hydrochloride resulted in distinct isolate-specific digestion patterns. Our CWD
isolates were also examined in protein misfolding cyclic amplification studies.
This showed different conversion activities for those isolates that had
displayed significantly different sensitivities to limited proteolysis by PK in
the biochemical experiments described above. We further applied Fourier
transform infrared spectroscopy in combination with atomic force microscopy.
This confirmed structural differences in the PrPTSE of at least two disinct CWD
isolates. The data presented here substantiate and expand previous reports on
the existence of different CWD strains.
2012
Envt.06:
Zoonotic Potential of CWD: Experimental
Transmissions to Non-Human Primates
Emmanuel Comoy,1,† Valérie Durand,1 Evelyne
Correia,1 Aru Balachandran,2 Jürgen Richt,3 Vincent Beringue,4 Juan-Maria
Torres,5 Paul Brown,1 Bob Hills6 and Jean-Philippe Deslys1
1Atomic Energy Commission; Fontenay-aux-Roses,
France; 2Canadian Food Inspection Agency; Ottawa, ON Canada; 3Kansas State
University; Manhattan, KS USA; 4INRA; Jouy-en-Josas, France; 5INIA; Madrid,
Spain; 6Health Canada; Ottawa, ON Canada
†Presenting author; Email: emmanuel.comoy@cea.fr
The constant increase of chronic wasting disease
(CWD) incidence in North America raises a question about their zoonotic
potential. A recent publication showed their transmissibility to new-world
monkeys, but no transmission to old-world monkeys, which are phylogenetically
closer to humans, has so far been reported. Moreover, several studies have
failed to transmit CWD to transgenic mice overexpressing human PrP. Bovine
spongiform encephalopathy (BSE) is the only animal prion disease for which a
zoonotic potential has been proven. We described the transmission of the
atypical BSE-L strain of BSE to cynomolgus monkeys, suggesting a weak
cattle-to-primate species barrier. We observed the same phenomenon with a
cattleadapted strain of TME (Transmissible Mink Encephalopathy). Since cattle
experimentally exposed to CWD strains have also developed spongiform
encephalopathies, we inoculated brain tissue from CWD-infected cattle to three
cynomolgus macaques as well as to transgenic mice overexpressing bovine or human
PrP. Since CWD prion strains are highly lymphotropic, suggesting an adaptation
of these agents after peripheral exposure, a parallel set of four monkeys was
inoculated with CWD-infected cervid brains using the oral route. Nearly four
years post-exposure, monkeys exposed to CWD-related prion strains remain
asymptomatic. In contrast, bovinized and humanized transgenic mice showed signs
of infection, suggesting that CWD-related prion strains may be capable of
crossing the cattle-to-primate species barrier. Comparisons with transmission
results and incubation periods obtained after exposure to other cattle prion
strains (c-BSE, BSE-L, BSE-H and cattle-adapted TME) will also be presented, in
order to evaluate the respective risks of each strain.
Envt.07:
Pathological Prion Protein (PrPTSE) in Skeletal
Muscles of Farmed and Free Ranging White-Tailed Deer Infected with Chronic
Wasting Disease
Martin L. Daus,1,† Johanna Breyer,2 Katjs
Wagenfuehr,1 Wiebke Wemheuer,2 Achim Thomzig,1 Walter Schulz-Schaeffer2 and
Michael Beekes1 1Robert Koch Institut; P24 TSE; Berlin, Germany; 2Department of
Neuropathology, Prion and Dementia Research Unit, University Medical Center
Göttingen; Göttingen, Germany †Presenting author; Email: dausm@rki.de
Chronic wasting disease (CWD) is a contagious,
rapidly spreading transmissible spongiform encephalopathy (TSE) occurring in
cervids 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 a direct biochemical demonstration of pathological
prion protein PrPTSE and of PrPTSE-associated seeding activity in skeletal
muscles of CWD-infected cervids. 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). The concentration of
PrPTSE in skeletal muscles of CWD-infected WTD was estimated to be approximately
2000- to 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.
CJD9/10022
October 1994
Mr R.N. Elmhirst Chairman British Deer Farmers
Association Holly Lodge Spencers Lane BerksWell Coventry CV7
7BZ
Dear Mr Elmhirst,
CREUTZFELDT-JAKOB DISEASE (CJD) SURVEILLANCE UNIT
REPORT
Thank you for your recent letter concerning the
publication of the third annual report from the CJD Surveillance Unit. I am
sorry that you are dissatisfied with the way in which this report was
published.
The Surveillance Unit is a completely independant
outside body and the Department of Health is committed to publishing their
reports as soon as they become available. In the circumstances it is not the
practice to circulate the report for comment since the findings of the report
would not be amended. In future we can ensure that the British Deer Farmers
Association receives a copy of the report in advance of
publication.
The Chief Medical Officer has undertaken to keep
the public fully informed of the results of any research in respect of CJD. This
report was entirely the work of the unit and was produced completely
independantly of the the Department.
The statistical results reqarding the consumption
of venison was put into perspective in the body of the report and was not
mentioned at all in the press release. Media attention regarding this report was
low key but gave a realistic presentation of the statistical findings of the
Unit. This approach to publication was successful in that consumption of venison
was highlighted only once by the media ie. in the News at one television
proqramme.
I believe that a further statement about the
report, or indeed statistical links between CJD and consumption of venison,
would increase, and quite possibly give damaging credence, to the whole issue.
From the low key media reports of which I am aware it seems unlikely that
venison consumption will suffer adversely, if at all.
now, let’s see what the authors said about this casual link, personal
communications years ago. see where it is stated NO STRONG evidence. so, does
this mean there IS casual evidence ????
“Our conclusion stating that we found no strong evidence of CWD
transmission to humans”
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
Sunday, November 10, 2002 6:26 PM ......snip........end..............TSS
Thursday, April 03, 2008
A prion disease of cervids: Chronic wasting disease
2008 1: Vet Res. 2008 Apr 3;39(4):41
A prion disease of cervids: Chronic wasting disease
Sigurdson CJ.
snip...
*** twenty-seven CJD patients who regularly consumed venison were reported
to the Surveillance Center***,
snip...
full text ;
Friday, November 09, 2012
*** Chronic Wasting Disease CWD in cervidae and transmission to other
species
Sunday, November 11, 2012
*** Susceptibilities of Nonhuman Primates to Chronic Wasting Disease
November 2012
Friday, December 14, 2012
Susceptibility Chronic Wasting Disease (CWD) in wild cervids to Humans 2005
- December 14, 2012
Saturday, March 09, 2013
*** Chronic Wasting Disease in Bank Voles: Characterisation of the Shortest
Incubation Time Model for Prion Diseases
*** NOR IS THE FDA recalling this CWD positive elk meat for the well being
of the dead elk ;
Wednesday, March 18, 2009 Noah’s Ark Holding, LLC, Dawson, MN RECALL Elk
products contain meat derived from an elk confirmed to have CWD NV, CA, TX, CO,
NY, UT, FL, OK RECALLS AND FIELD CORRECTIONS: FOODS CLASS II
___________________________________
PRODUCT
a) Elk Meat, Elk Tenderloin, Frozen in plastic vacuum packaging. Each
package is approximately 2 lbs., and each case is approximately 16 lbs.; Item
number 755125, Recall # F-129-9;
b) Elk Meat, Elk Trim, Frozen; Item number 755155, Recall # F-130-9;
c) Elk Meat, French Rack, Chilled. Item number 755132, Recall #
F-131-9;
d) Elk Meat, Nude Denver Leg. Item number 755122, Recall # F-132-9;
e) Elk Meat, New York Strip Steak, Chilled. Item number 755128, Recall #
F-133-9;
f) Elk Meat, Flank Steak Frozen. Item number 755131, Recall #
F-134-9;
CODE
Elk Meats with production dates of December 29, 30, and 31
RECALLING FIRM/MANUFACTURER
Recalling Firm: Sierra Meats, Reno, NV, by telephone on January 29, 2009
and press release on February 9, 2009.
Manufacturer: Noah’s Ark Holding, LLC, Dawson, MN. Firm initiated recall is
ongoing.
REASON
Elk products contain meat derived from an elk confirmed to have Chronic
Wasting Disease (CWD).
VOLUME OF PRODUCT IN COMMERCE
Unknown
DISTRIBUTION
NV, CA, TX, CO, NY, UT, FL, OK
___________________________________
Monday, February 09, 2009
Exotic Meats USA Announces Urgent Statewide Recall of Elk Tenderloin
Because It May Contain Meat Derived From An Elk Confirmed To Have CWD
snip...
Cross-sequence transmission of sporadic Creutzfeldt-Jakob disease creates a
new prion strain
Date: August 25, 2007 at 12:42 pm PST
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.
Wednesday, March 18, 2009
Noah's Ark Holding, LLC, Dawson, MN RECALL Elk products contain meat
derived from an elk confirmed to have CWD NV, CA, TX, CO, NY, UT, FL, OK RECALLS
AND FIELD CORRECTIONS: FOODS CLASS II
Friday, December 14, 2012
DEFRA U.K. What is the risk of Chronic Wasting Disease CWD being introduced
into Great Britain? A Qualitative Risk Assessment October 2012
New studies on the heat resistance of hamster-adapted scrapie agent:
Threshold survival after ashing at 600°C suggests an inorganic template of
replication
Prion Infected Meat-and-Bone Meal Is Still Infectious after Biodiesel
Production
Detection of protease-resistant cervid prion protein in water from a
CWD-endemic area
A Quantitative Assessment of the Amount of Prion Diverted to Category 1
Materials and Wastewater During Processing
Rapid assessment of bovine spongiform encephalopathy prion inactivation by
heat treatment in yellow grease produced in the industrial manufacturing process
of meat and bone meals
PPo4-4:
Survival and Limited Spread of TSE Infectivity after Burial
CWD, CJD, TSE PRION, it’s not just about you and your family, it’s about
all of us, my family and yours. consumption is but only one route. the pass if
forward, friendly fire, iatrogenic threat is REAL !!!
Tuesday, February 11, 2014
Novant Health Forsyth Medical Center Information on potential CJD exposure
kind regards,
terry
posted by Terry S. Singeltary Sr. at
5:07 PM
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