scholarly journals Evidence for distinct chronic wasting disease (CWD) strains in experimental CWD in ferrets

2012 ◽  
Vol 93 (1) ◽  
pp. 212-221 ◽  
Author(s):  
Matthew R. Perrott ◽  
Christina J. Sigurdson ◽  
Gary L. Mason ◽  
Edward A. Hoover
Keyword(s):  
North America ◽  
Chronic Wasting Disease ◽  
Proteinase K ◽  
Clinical Progression ◽  
Mustela Putorius ◽  
Wasting Disease ◽  
Experimental Inoculation ◽  
Distinct Strain ◽  
Transport Species ◽  
The Brain

Chronic wasting disease (CWD) is an evolving prion disease of cervids (deer, elk and moose) that has been recognized in North America and Korea. Infection of non-cervid reservoir or transport species in nature is not reported. However, the ferret (Mustela putorius furo) is susceptible to CWD after experimental inoculation. Here, we report that infection of ferrets with either of two ferret CWD isolates by various routes of exposure has revealed biologically distinct strain-like properties distinguished by different clinical progression and survival period. The isolates of ferret CWD were also differentiated by the distribution of the infectious prion protein (PrPCWD) in the brain and periphery, and by the proteinase K sensitivity of PrPCWD. These findings suggest that diversity in prion conformers exists in CWD-infected cervids.

scholarly journals Survey of Cattle in Northeast Colorado for Evidence of Chronic Wasting Disease: Geographical and High-Risk Targeted Sample

2003 ◽  
Vol 15 (3) ◽  
pp. 274-277 ◽  
Author(s):  
Daniel H. Gould ◽  
James L. Voss ◽  
Michael W. Miller ◽  
Annette M. Bachand ◽  
Bruce A. Cummings ◽  
...  
Keyword(s):  
High Risk ◽  
Large Scale ◽  
Chronic Wasting Disease ◽  
Transmissible Spongiform Encephalopathy ◽  
Proteinase K ◽  
Spongiform Encephalopathy ◽  
Wasting Disease ◽  
Adult Cattle ◽  
Endemic Areas ◽  
Geographically Targeted

A geographically targeted survey of potentially high-risk, adult cattle in chronic wasting disease (CWD)–endemic areas in Colorado was initiated to assess the possibility of the spread of CWD from deer to cattle under natural conditions. Surveyed cattle were sympatric with free-roaming deer in geographically defined areas where CWD occurs and where CWD prevalence has been estimated. To qualify for inclusion in the survey, cattle had to be at least 4 years old and had to have spent a minimum of 4 years in surveyed areas. Brains from culled cattle were examined microscopically and immunohistochemically for tissue alterations indicative of a transmissible spongiform encephalopathy (TSE). Two hundred sixty-two brains were suitable for evaluation and were found to lack changes indicative of a TSE infection. Prion deposition was not demonstrable using a method involving formic acid and proteinase-K treatment before application of monoclonal antibody to bovine prion protein (F99/97.6.1). Some incidental neuropathologic changes unrelated to those of TSEs were detected. Findings from this study suggest that large-scale spread of CWD from deer to cattle under natural range conditions in CWD-endemic areas of northeast Colorado is unlikely.

scholarly journals Studies in bank voles reveal strain differences between chronic wasting disease prions from Norway and North America

2020 ◽  
Vol 117 (49) ◽  
pp. 31417-31426 ◽  
Author(s):  
Romolo Nonno ◽  
Michele A. Di Bari ◽  
Laura Pirisinu ◽  
Claudia D’Agostino ◽  
Ilaria Vanni ◽  
...  
Keyword(s):  
North America ◽  
North American ◽  
Rangifer Tarandus ◽  
Chronic Wasting Disease ◽  
Strain Differences ◽  
Myodes Glareolus ◽  
Wasting Disease ◽  
Proximate Cause ◽  
Bank Voles ◽  
Regional Deposition

Chronic wasting disease (CWD) is a relentless epidemic disorder caused by infectious prions that threatens the survival of cervid populations and raises increasing public health concerns in North America. In Europe, CWD was detected for the first time in wild Norwegian reindeer (Rangifer tarandus) and moose (Alces alces) in 2016. In this study, we aimed at comparing the strain properties of CWD prions derived from different cervid species in Norway and North America. Using a classical strain typing approach involving transmission and adaptation to bank voles (Myodes glareolus), we found that prions causing CWD in Norway induced incubation times, neuropathology, regional deposition of misfolded prion protein aggregates in the brain, and size of their protease-resistant core, different from those that characterize North American CWD. These findings show that CWD prion strains affecting Norwegian cervids are distinct from those found in North America, implying that the highly contagious North American CWD prions are not the proximate cause of the newly discovered Norwegian CWD cases. In addition, Norwegian CWD isolates showed an unexpected strain variability, with reindeer and moose being caused by different CWD strains. Our findings shed light on the origin of emergent European CWD, have significant implications for understanding the nature and the ecology of CWD in Europe, and highlight the need to assess the zoonotic potential of the new CWD strains detected in Europe.

Differentially expressed genes in the brain of TgElk mice with chronic wasting disease

2016 ◽  
Vol 40 (4) ◽  
pp. 120-126
Author(s):  
Hyo-Jin Kim ◽  
◽  
In Soon Roh ◽  
Min-Jeong Kim ◽  
Dong-Seob Tark ◽  
...  
Keyword(s):  
Differentially Expressed Genes ◽  
Chronic Wasting Disease ◽  
Differentially Expressed ◽  
Wasting Disease ◽  
The Brain

Rapid Procedure For Detecting Scrapie-Associated Fibrils In Chronic Wasting Disease Of Elk And Mule Deer

1999 ◽  
Vol 5 (S2) ◽  
pp. 1310-1311
Author(s):  
C.E. Hearne ◽  
J.L. Clapper ◽  
K.L. DeVries ◽  
E.S. Williams
Keyword(s):  
High Speed ◽  
Chronic Wasting Disease ◽  
Transmissible Spongiform Encephalopathy ◽  
Mule Deer ◽  
Proteinase K ◽  
Abnormal Behavior ◽  
Enzyme Treatment ◽  
Spongiform Encephalopathy ◽  
Wasting Disease ◽  
Gradual Loss

Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) of mule deer and elk. Affected animals are characterized clinically by a combination of abnormal behavior and gradual loss of body condition. The disease is invariably fatal. Diagnosis of CWD is made by histologic examination of the central nervous system and microscopic lesions of CWD are typical of the TSEs. Brains from CWD-suspect elk and mule deer can be examined by transmission electron microscopy (TEM) for the presence of scrapie-associated fibrils (SAF). Western blot methods identify abnormal prion protein (PrPres) which accumulates in the brains of animals with TSE, including CWD.Conventional SAF purification procedures for TEM examination of CWD-suspect brain tissue require both high speed and ultracentrifugation steps followed by Proteinase K enzyme treatment. Modifications used in this experiment include early Proteinase K, or Proteinase K and Collagenase treatment prior to high speed centrifugation and the elimination of the ultracentrifugation step.

scholarly journals Strain Fidelity of Chronic Wasting Disease upon Murine Adaptation

2006 ◽  
Vol 80 (24) ◽  
pp. 12303-12311 ◽  
Author(s):  
Christina J. Sigurdson ◽  
Giuseppe Manco ◽  
Petra Schwarz ◽  
Pawel Liberski ◽  
Edward A. Hoover ◽  
...  
Keyword(s):  
North America ◽  
Transgenic Mice ◽  
Chronic Wasting Disease ◽  
Amyloid Plaques ◽  
Serial Passage ◽  
Host Factors ◽  
Species Barrier ◽  
Wasting Disease ◽  
Cerebral Amyloid ◽  
Efficient Transmission

ABSTRACT Chronic wasting disease (CWD), a prion disease of deer and elk, is highly prevalent in some regions of North America. The establishment of mouse-adapted CWD prions has proven difficult due to the strong species barrier between mice and deer. Here we report the efficient transmission of CWD to transgenic mice overexpressing murine PrP. All mice developed disease 500 ± 62 days after intracerebral CWD challenge. The incubation period decreased to 228 ± 103 days on secondary passage and to 162 ± 6 days on tertiary passage. Mice developed very large, radially structured cerebral amyloid plaques similar to those of CWD-infected deer and elk. PrPSc was detected in spleen, indicating that murine CWD was lymphotropic. PrPSc glycoform profiles maintained a predominantly diglycosylated PrP pattern, as seen with CWD in deer and elk, across all passages. Therefore, all pathological, biochemical, and histological strain characteristics of CWD appear to persist upon repetitive serial passage through mice. These findings indicate that the salient strain-specific properties of CWD are encoded by agent-intrinsic components rather than by host factors.

scholarly journals Detection of Chronic Wasting Disease Prions in Fetal Tissues of Free-Ranging White-Tailed Deer

Viruses ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 2430
Author(s):  
Amy V. Nalls ◽  
Erin E. McNulty ◽  
Amber Mayfield ◽  
James M. Crum ◽  
M. Kevin Keel ◽  
...  
Keyword(s):  
North America ◽  
Vertical Transmission ◽  
Protein Misfolding ◽  
Chronic Wasting Disease ◽  
Wasting Disease ◽  
Indirect Contact ◽  
Fetal Tissues ◽  
Animal Exposure ◽  
Asymptomatic Phase ◽  
Free Ranging

The transmission of chronic wasting disease (CWD) has largely been attributed to contact with infectious prions shed in excretions (saliva, urine, feces, blood) by direct animal-to-animal exposure or indirect contact with the environment. Less-well studied has been the role that mother-to-offspring transmission may play in the facile transmission of CWD, and whether mother-to-offspring transmission before birth may contribute to the extensive spread of CWD. We thereby focused on a population of free-ranging white-tailed deer from West Virginia, USA, in which CWD has been detected. Fetal tissues, ranging from 113 to 158 days of gestation, were harvested from the uteri of CWD+ dams in the asymptomatic phase of infection. Using serial protein misfolding amplification (sPMCA), we detected evidence of prion seeds in 7 of 14 fetuses (50%) from 7 of 9 pregnancies (78%), with the earliest detection at 113 gestational days. This is the first report of CWD detection in free ranging white-tailed deer fetal tissues. Further investigation within cervid populations across North America will help define the role and impact of mother-to-offspring vertical transmission of CWD.

scholarly journals New and distinct chronic wasting disease strains associated with cervid polymorphism at codon 116 of the Prnp gene

2021 ◽  
Vol 17 (7) ◽  
pp. e1009795
Author(s):  
Samia Hannaoui ◽  
Elizabeth Triscott ◽  
Camilo Duque Velásquez ◽  
Sheng Chun Chang ◽  
Maria Immaculata Arifin ◽  
...  
Keyword(s):  
Prion Protein ◽  
Chronic Wasting Disease ◽  
Prnp Gene ◽  
Biochemical Properties ◽  
Cellular Prion Protein ◽  
Proteinase K ◽  
Wild Type ◽  
Wasting Disease ◽  
Prion Strains ◽  
The Impact

Chronic wasting disease (CWD) is a prion disease affecting cervids. Polymorphisms in the prion protein gene can result in extended survival of CWD-infected animals. However, the impact of polymorphisms on cellular prion protein (PrPC) and prion properties is less understood. Previously, we characterized the effects of a polymorphism at codon 116 (A>G) of the white-tailed deer (WTD) prion protein and determined that it destabilizes PrPC structure. Comparing CWD isolates from WTD expressing homozygous wild-type (116AA) or heterozygous (116AG) PrP, we found that 116AG-prions were conformationally less stable, more sensitive to proteases, with lower seeding activity in cell-free conversion and reduced infectivity. Here, we aimed to understand CWD strain emergence and adaptation. We show that the WTD-116AG isolate contains two different prion strains, distinguished by their host range, biochemical properties, and pathogenesis from WTD-116AA prions (Wisc-1). Serial passages of WTD-116AG prions in tg(CerPrP)1536+/+ mice overexpressing wild-type deer-PrPC revealed two populations of mice with short and long incubation periods, respectively, and remarkably prolonged clinical phase upon inoculation with WTD-116AG prions. Inoculation of serially diluted brain homogenates confirmed the presence of two strains in the 116AG isolate with distinct pathology in the brain. Interestingly, deglycosylation revealed proteinase K-resistant fragments with different electrophoretic mobility in both tg(CerPrP)1536+/+ mice and Syrian golden hamsters infected with WTD-116AG. Infection of tg60 mice expressing deer S96-PrP with 116AG, but not Wisc-1 prions induced clinical disease. On the contrary, bank voles resisted 116AG prions, but not Wisc-1 infection. Our data indicate that two strains co-existed in the WTD-116AG isolate, expanding the variety of CWD prion strains. We argue that the 116AG isolate does not contain Wisc-1 prions, indicating that the presence of 116G-PrPC diverted 116A-PrPC from adopting a Wisc-1 structure. This can have important implications for their possible distinct capacities to cross species barriers into both cervids and non-cervids.

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