The importance of localized culling in stabilizing chronic wasting disease prevalence in white-tailed deer populations
Mateus-Pinilla Jan Novakofski PII: S0167-5877(13)00289-4 DOI: http://dx.doi.org/doi:10.1016/j.prevetmed.2013.09.011
Reference: PREVET 3436 To appear in: PREVET
Received date: 11-12-2012 Revised date: 11-9-2013 Accepted date: 14-9-2013
Please cite this article as: Manjerovic, M.B., Green, M.L., Mateus-Pinilla,
N., Novakofski, J.,
The importance of localized culling in stabilizing chronic wasting disease
prevalence in white-tailed deer populations, Preventive Veterinary Medicine
(2013), http://dx.doi.org/10.1016/j.prevetmed.2013.09.011
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Page 1 of 27
Accepted Manuscript
The importance of localized culling in stabilizing chronic wasting disease
prevalence in white-tailed deer populations
Mary Beth Manjerovic1,2, Michelle L. Green1,2, Nohra Mateus-Pinilla1, and
Jan Novakofski2
1Illinois Natural History Survey, University of Illinois Urbana-Champaign,
1816 S. Oak Street, Champaign, IL, 61820, USA
2Department of Animal Sciences, Illinois Natural History Survey, University
of Illinois Urbana-Champaign, 1503 S. Maryland Drive, Urbana, IL, 61801, USA
Corresponding author: Nohra Mateus-Pinilla Phone: 1-217-333-6856 Fax:
1-217-244-0802 Email: nohram@illinois.edu
Correspondence address: Illinois Natural History Survey University of
Illinois Urbana-Champaign 1816 S. Oak Street Champaign, IL, 61820, USA
nohram@illinois.edu
Page 2 of 27 Accepted Manuscript
Abstract
Strategies to contain the spread of disease often are developed with
incomplete knowledge of the possible outcomes but are intended to minimize the
risks associated with delaying control. Culling of game species by government
agencies is one approach to control disease in wild populations but is unpopular
with hunters and wildlife enthusiasts, politically unpalatable, and erodes
public support for agencies responsible for wildlife management. We addressed
the functional differences between hunting and government culling programs for
managing chronic wasting disease (CWD) in white39 tailed deer by comparing
prevalence over a 10-year period in Illinois and Wisconsin. We found similar
prevalence in both states when management emphasized culling but an increase in
CWD after Wisconsin switched from culling to a hunter-harvest focused management
strategy. Despite its unpopularity among hunters, localized culling is a disease
management strategy that can maintain low disease prevalence without affecting
recreational deer harvest.
Keywords: culling, prion, chronic wasting disease, white-tailed deer,
wildlife, prevalence, disease management
snip...
Introduction
North American cervids [mule deer (Odocoileus hemionus), elk (Cervus
elaphus), moose (Alces alces), and white-tailed deer (Odocoileus virginianus)]
are popular game animals making them economically and recreationally valuable
species. Free-living cervids are susceptible to chronic wasting disease (CWD)
(Miller et al. 2000; Spraker et al. 1997), a contagious and fatal prion disease
with no cure or treatment (Williams et al., 2002). To date, CWD has been
identified in free-ranging cervid populations in 17 states and two Canadian
provinces (http://www.nwhc.usgs.gov/disease_information/chronic_wasting_disease/index.jsp).
CWD is spread in free-living animals through contact with bodily secretions or
infectious agents persisting in contaminated environments (Mathiason et al.,
2009, 2006; Walter et al., 2011; Williams et al., 2002). Such transmissibility
results in a self-sustaining CWD epizootic with prevalence increasing slowly
over time (Miller et al., 2000; Miller and Conner, 2005; Saunders et al., 2012;
Williams et al., 2002). Furthermore, the environmental load of infectious prions
increases with the number of infectious animals making CWD exceedingly difficult
to eliminate from free-ranging populations once established (Almberg et al.,
2011; Gross and Miller, 2001). CWD models suggest substantial declines in cervid
populations with high prevalence and highlight the importance of long-term,
sustained management programs in controlling CWD (Gross and Miller, 2001;
Mateus-Pinilla et al., 2013; Wasserberg et al., 2009). ...
snip...see full text ;
abstract
see full text ;
Friday, September 27, 2013
Uptake of Prions into Plants
Presentation Abstract
Prion2013
Friday, August 09, 2013
***CWD TSE prion, plants, vegetables, and the potential for environmental
contamination
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?
PRION2013 CONGRESSIONAL ABSTRACTS CWD
Thursday, August 08, 2013
Characterization of the first case of naturally occurring chronic wasting
disease in a captive red deer (Cervus elaphus) in North America
Wednesday, September 04, 2013
***cwd - cervid captive livestock escapes, loose and on the run in the
wild...
Tuesday, September 10, 2013
Review and Updates of the USDA-APHIS Veterinary Services (VS) National
Chronice Wasting Disease (CWD) Program 2012-2013
Sunday, August 11, 2013
Creutzfeldt-Jakob Disease CJD cases rising North America updated report
August 2013
Creutzfeldt-Jakob Disease CJD cases rising North America with Canada seeing
an extreme increase of 48% between 2008 and 2010
*** 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.
kind regards, terry
posted by Terry S. Singeltary Sr. at
9:31 PM
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