Journal of Veterinary Medical Science Article ID: 13-0363 Language: English
Japanese Previous Article |Next Article http://dx.doi.org/10.1292/jvms.13-0363
DN/JST.JSTAGE/jvms/13-0363
Advance Publication
The Presence of Disease-Associated Prion Protein in Skeletal Muscle of
Cattle Infected with Classical Bovine Spongiform Encephalopathy
Hiroyuki OKADA1), Kohtaro MIYAZAWA1), Shigeo FUKUDA2), Yoshifumi IWAMARU1),
Morikazu IMAMURA1), Kentaro MASUJIN1), Yuichi MATSUURA1), Takashi FUJII2), Kei
FUJII2), Soichi KAGEYAMA2), Miyako YOSHIOKA1), Yuichi MURAYAMA1), Takashi
YOKOYAMA1)
1) National Institute of Animal Health, National Agriculture and Food
Research Organization 2) Hokkaido Animal Research Center, Hokkaido Research
Organization
[Advance Publication] Released 2013/08/27 received 2013/07/16 accepted
2013/08/13 Keywords: BSE, muscle spindle, prion, skeletal muscle
Full Text PDF [832K]
Abstracts
The aim of this study was to investigate the presence of disease-associated
prion protein (PrPSc) in the skeletal muscle of cattle infected with classical
bovine spongiform encephalopathy (C-BSE). The study was carried out
systematically in 12 different muscle samples from 43 (3 field and 40
experimental) cases of C-BSE; however, muscle spindles were not available in
many of these cases. Therefore, analysis became restricted to a total of 31
muscles in 23 cattle. Even after this restriction, low levels of PrPSc were
detected in the muscle spindles of the masseter, intercostal, triceps brachii,
psoas major, quadriceps femoris and semitendinosus muscles from 3 field and 6
experimental clinical-stage cases. The present data indicate that small amounts
of PrPSc are detectable by immunohistochemistry in the skeletal muscles of
animals terminally affected with C-BSE.
full text pdf here ;
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Infectivity in Skeletal Muscle of Cattle with Atypical Bovine Spongiform
Encephalopathy PLoS One. 2012; 7(2): e31449.
***Infectivity in skeletal muscle of BASE-infected cattle
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Biochemical Characteristics and PrPSc Distribution Pattern in the Brains of
Cattle Experimentally Challenged with H-type and L-type Atypical BSE
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Stability properties of PrPSc from cattle with experimental transmissible
spongiform encephalopathies: use of a rapid whole homogenate, protease-free
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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.
http://www.landesbioscience.com/journals/prion/Prion5-Supp-PrionEnvironment.pdf?nocache=1333529975
Wednesday, April 06, 2011
Presence and Seeding Activity of Pathological Prion Protein (PrPTSE) in
Skeletal Muscles of White-Tailed Deer Infected with Chronic Wasting Disease
Sunday, November 21, 2010
Preclinical Deposition of Pathological Prion Protein in Muscle of
Experimentally Infected Primates and potential Iatrogenic TSE there from
Preclinical Deposition of Pathological Prion Protein in Muscle of Experimentally
Infected Primates
EMBO reports AOP Published online: 11 April 2003
Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie
Achim Thomzig, Christine Kratzel, Gudrun Lenz, Dominique KrÒ¼ger & Michael Beekes Robert Koch-Institut, P26, Nordufer 20, D-13353 Berlin, Germany
Received 13 February 2003; Accepted 13 March 2003; Published online 11 April 2003.
Abstract :
Scrapie, bovine spongiform encephalopathy and chronic wasting disease are orally communicable, transmissible spongiform encephalopathies (TSEs). As zoonotic transmissions of TSE agents may pose a risk to human health, the identification of reservoirs for infectivity in animal tissues and their exclusion from human consumption has become a matter of great importance for consumer protection. In this study, a variety of muscles from hamsters that were orally challenged with scrapie was screened for the presence of a molecular marker for TSE infection, PrPSc (the pathological isoform of the prion protein PrP). Sensitive western blotting revealed consistent PrPSc accumulation in skeletal muscles from forelimb and hindlimb, head, back and shoulder, and in tongue. Previously, our animal model has provided substantial baseline information about the peripheral routing of infection in naturally occurring and orally acquired ruminant TSEs. Therefore, the findings described here highlight further the necessity to investigate thoroughly whether muscles of TSE-infected sheep, cattle, elk and deer contain infectious agents.
http://www.emboreports.org/
snip...see;
Monday, June 22, 2009
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