Differing Neurohistologic Images of Scrapie, Transmissible Mink Encephalopathy, and Chronic Wasting Disease of Mule Deer and Elk

1996 ◽  
pp. 122-137 ◽  
Author(s):  
William J. Hadlow
2005 ◽  
Vol 41 (4) ◽  
pp. 820-824 ◽  
Author(s):  
Krysten L. Schuler ◽  
Jonathan A. Jenks ◽  
Christopher S. DePerno ◽  
Margaret A. Wild ◽  
Christopher C. Swanson

mSphere ◽  
2020 ◽  
Vol 5 (5) ◽  
Author(s):  
Ronald A. Shikiya ◽  
Anthony E. Kincaid ◽  
Jason C. Bartz ◽  
Travis J. Bourret

ABSTRACT Chronic wasting disease (CWD) is an emerging and fatal contagious prion disease that affects cervids, including mule deer, white-tailed deer, black-tailed deer, red deer reindeer, elk, and moose. CWD prions are widely distributed throughout the bodies of CWD-infected animals and are found in the nervous system, lymphoid tissues, muscle, blood, urine, feces, and antler velvet. The mechanism of CWD transmission in natural settings is unknown. Potential mechanisms of transmission include horizontal, maternal, or environmental routes. Due to the presence of prions in the blood of CWD-infected animals, the potential exists for invertebrates that feed on mammalian blood to contribute to the transmission of CWD. The geographic range of the Rocky Mountain Wood tick, Dermancentor andersoni, overlaps with CWD throughout the northwest United States and southwest Canada, raising the possibility that D. andersoni parasitization of cervids may be involved in CWD transmission. We investigated this possibility by examining the blood meal of D. andersoni that fed upon prion-infected hamsters for the presence of prion infectivity by animal bioassay. None of the hamsters inoculated with a D. andersoni blood meal that had been ingested from prion-infected hamsters developed clinical signs of prion disease or had evidence for a subclinical prion infection. Overall, the data do not demonstrate a role for D. andersoni in the transmission of prion disease. IMPORTANCE Chronic wasting disease (CWD) is an emerging prion disease that affects cervids, including mule deer, white-tailed deer, black-tailed deer, red deer reindeer, elk, and moose. The mechanism of CWD transmission in unknown. Due to the presence of prions in the blood of CWD-infected animals, it is possible for invertebrates that feed on cervid blood to contribute to the transmission of CWD. We examined the blood meal of D. andersoni, a tick with a similar geographic range as cervids, that fed upon prion-infected hamsters for the presence of prion infectivity by animal bioassay. None of the D. andersoni blood meals that had been ingested from prion-infected hamsters yielded evidence of prion infection. Overall, the data do not support a role of D. andersoni in the transmission of prion disease.


Ecosphere ◽  
2018 ◽  
Vol 9 (1) ◽  
Author(s):  
María Fernanda Mejía‐Salazar ◽  
Cheryl L. Waldner ◽  
Yeen Ten Hwang ◽  
Trent K. Bollinger

2001 ◽  
Vol 13 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Amir N. Hamir ◽  
Randall C. Cutlip ◽  
Janice M. Miller ◽  
Elizabeth S. Williams ◽  
Mick J. Stack ◽  
...  

1993 ◽  
Vol 85 (4) ◽  
pp. 437-444 ◽  
Author(s):  
Don C. Guiroy ◽  
Elizabeth S. Williams ◽  
Pawel P. Liberski ◽  
Ikuro Wakayama ◽  
D. Carleton Gajdusek

ACS Omega ◽  
2019 ◽  
Vol 4 (22) ◽  
pp. 19913-19924 ◽  
Author(s):  
Urška Slapšak ◽  
Giulia Salzano ◽  
Gregor Ilc ◽  
Gabriele Giachin ◽  
Jifeng Bian ◽  
...  

2007 ◽  
Vol 19 (6) ◽  
pp. 680-686 ◽  
Author(s):  
Amir N. Hamir ◽  
Robert A. Kunkle ◽  
Janice M. Miller ◽  
Randall C. Cutlip ◽  
Juergen A. Richt ◽  
...  

2006 ◽  
Vol 80 (2) ◽  
pp. 596-604 ◽  
Author(s):  
Gregory J. Raymond ◽  
Emily A. Olsen ◽  
Kil Sun Lee ◽  
Lynne D. Raymond ◽  
P. Kruger Bryant ◽  
...  

ABSTRACT Chronic wasting disease (CWD) is an emerging transmissible spongiform encephalopathy (prion disease) of North American cervids, i.e., mule deer, white-tailed deer, and elk (wapiti). To facilitate in vitro studies of CWD, we have developed a transformed deer cell line that is persistently infected with CWD. Primary cultures derived from uninfected mule deer brain tissue were transformed by transfection with a plasmid containing the simian virus 40 genome. A transformed cell line (MDB) was exposed to microsomes prepared from the brainstem of a CWD-affected mule deer. CWD-associated, protease-resistant prion protein (PrPCWD) was used as an indicator of CWD infection. Although no PrPCWD was detected in any of these cultures after two passes, dilution cloning of cells yielded one PrPCWD-positive clone out of 51. This clone, designated MDBCWD, has maintained stable PrPCWD production through 32 serial passes thus far. A second round of dilution cloning yielded 20 PrPCWD-positive subclones out of 30, one of which was designated MDBCWD2. The MDBCWD2 cell line was positive for fibronectin and negative for microtubule-associated protein 2 (a neuronal marker) and glial fibrillary acidic protein (an activated astrocyte marker), consistent with derivation from brain fibroblasts (e.g., meningeal fibroblasts). Two inhibitors of rodent scrapie protease-resistant PrP accumulation, pentosan polysulfate and a porphyrin compound, indium (III) meso-tetra(4-sulfonatophenyl)porphine chloride, potently blocked PrPCWD accumulation in MDBCWD cells. This demonstrates the utility of these cells in a rapid in vitro screening assay for PrPCWD inhibitors and suggests that these compounds have potential to be active against CWD in vivo.


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