Immunologic and Molecular Biologic Studies of Prion Proteins in Bovine Spongiform Encephalopathy

1993 ◽  
Vol 167 (3) ◽  
pp. 602-613 ◽  
Author(s):  
S. B. Prusiner ◽  
M. Fuzi ◽  
M. Scott ◽  
D. Serban ◽  
H. Serban ◽  
...  
2009 ◽  
Vol 90 (3) ◽  
pp. 764-768 ◽  
Author(s):  
Michael Stack ◽  
Lorenzo González ◽  
Martin Jeffrey ◽  
Stuart Martin ◽  
Colin Macaldowie ◽  
...  

During the 1980s, bovine spongiform encephalopathy (BSE)-contaminated meat and bonemeal were probably fed to sheep, raising concerns that BSE may have been transmitted to sheep in the UK. The human disease, variant Creutzfeldt–Jakob disease, arose during the BSE epidemic, and oral exposure of humans to BSE-infected tissues has been implicated in its aetiology. The concern is that sheep BSE could provide another source of BSE exposure to humans via sheep products. Two immunological techniques, Western immunoblotting (WB) and immunohistochemistry (IHC), have been developed to distinguish scrapie from cases of experimental sheep BSE by the characteristics of their respective abnormal, disease-associated prion proteins (PrPd). This study compares the WB and IHC characteristics of PrPd from brains of primary, secondary and tertiary experimental ovine BSE cases with those of cattle BSE and natural sheep scrapie. Discrimination between experimental sheep BSE and scrapie remained possible by both methods, regardless of the route of challenge.


2014 ◽  
Author(s):  
Noboru Manabe ◽  
Ichiro Onoyama ◽  
Junyou Li ◽  
Yutaka Sendai ◽  
Yoshito Aoyagi

1997 ◽  
Vol 141 (14) ◽  
pp. 352-357 ◽  
Author(s):  
A. R. Austin ◽  
L. Pawson ◽  
S. Meek ◽  
S. Webster

Prion ◽  
2021 ◽  
Vol 15 (1) ◽  
pp. 1-11
Author(s):  
Sandor Dudas ◽  
Renee Anderson ◽  
Antanas Staskevicus ◽  
Gordon Mitchell ◽  
James C. Cross ◽  
...  

1993 ◽  
Vol 34 (1) ◽  
pp. 99-100
Author(s):  
J. S. Agerholm ◽  
H. V. Krogh ◽  
T. K. Nielsen ◽  
S. Ammendrup ◽  
H. Dalsgaard

2013 ◽  
Vol 94 (12) ◽  
pp. 2819-2827 ◽  
Author(s):  
Rona Wilson ◽  
Karen Dobie ◽  
Nora Hunter ◽  
Cristina Casalone ◽  
Thierry Baron ◽  
...  

The transmission of bovine spongiform encephalopathy (BSE) to humans, leading to variant Creutzfeldt–Jakob disease has demonstrated that cattle transmissible spongiform encephalopathies (TSEs) can pose a risk to human health. Until recently, TSE disease in cattle was thought to be caused by a single agent strain, BSE, also known as classical BSE, or BSE-C. However, due to the initiation of a large-scale surveillance programme throughout Europe, two atypical BSE strains, bovine amyloidotic spongiform encephalopathy (BASE, also named BSE-L) and BSE-H have since been discovered. To model the risk to human health, we previously inoculated these two forms of atypical BSE (BASE and BSE-H) into gene-targeted transgenic (Tg) mice expressing the human prion protein (PrP) (HuTg) but were unable to detect any signs of TSE pathology in these mice. However, despite the absence of TSE pathology, upon subpassage of some BASE-challenged HuTg mice, a TSE was observed in recipient gene-targeted bovine PrP Tg (Bov6) mice but not in HuTg mice. Disease transmission from apparently healthy individuals indicates the presence of subclinical BASE infection in mice expressing human PrP that cannot be identified by current diagnostic methods. However, due to the lack of transmission to HuTg mice on subpassage, the efficiency of mouse-to-mouse transmission of BASE appears to be low when mice express human rather than bovine PrP.


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