scholarly journals Detection of PrPBSE and prion infectivity in the ileal Peyer’s patch of young calves as early as 2 months after oral challenge with classical bovine spongiform encephalopathy

2017 ◽  
Vol 48 (1) ◽  
Author(s):  
Ivett Ackermann ◽  
Anne Balkema-Buschmann ◽  
Reiner Ulrich ◽  
Kerstin Tauscher ◽  
James C. Shawulu ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Oral Challenge ◽  
Spongiform Encephalopathy ◽  
Peyer’S Patch ◽  
Peyer's Patch ◽  
Prion Infectivity ◽  
Classical Bovine Spongiform Encephalopathy

scholarly journals Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys

2014 ◽  
Vol 95 (7) ◽  
pp. 1612-1618 ◽  
Author(s):  
Pedro Piccardo ◽  
Juraj Cervenak ◽  
Ming Bu ◽  
Lindsay Miller ◽  
David M. Asher
Keyword(s):  
Neurodegenerative Diseases ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Common Mechanism ◽  
Spongiform Encephalopathy ◽  
Hyperphosphorylated Tau ◽  
Jakob Disease ◽  
Spongiform Degeneration ◽  
Bovine Spongiform Encephalopathy Agent ◽  
Classical Bovine Spongiform Encephalopathy

Proteins aggregate in several slowly progressive neurodegenerative diseases called ‘proteinopathies’. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well – a possible common mechanism for some neurodegenerative diseases. However, most proteinopathies are ‘sporadic’, without gene mutation or overexpression. Thus, proteinopathies in WT animals genetically close to humans might be informative. Squirrel monkeys infected with the classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant Creutzfeldt–Jakob disease with accumulations not only of abnormal prion protein (PrPTSE), but also three other proteins: hyperphosphorylated tau (p-tau), α-synuclein and ubiquitin; β-amyloid protein (Aβ) did not accumulate. Severity of brain lesions correlated with spongiform degeneration. No amyloid was detected. These results suggested that PrPTSE enhanced formation of p-tau and aggregation of α-synuclein and ubiquitin, but not Aβ, providing a new experimental model for neurodegenerative diseases associated with complex proteinopathies.

Polymorphism of the prion protein gene (PRNP) in Polish cattle affected by classical bovine spongiform encephalopathy

2011 ◽  
Vol 39 (5) ◽  
pp. 5211-5217 ◽  
Author(s):  
Artur Gurgul ◽  
Czarnik Urszula ◽  
Magdalena Larska ◽  
Mirosław P. Polak ◽  
Janusz Strychalski ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Classical Bovine Spongiform Encephalopathy

Tissue distribution of bovine spongiform encephalopathy infectivity in Romney sheep up to the onset of clinical disease after oral challenge

2005 ◽  
Vol 156 (7) ◽  
pp. 197-202 ◽  
Author(s):  
S. J. Bellworthy ◽  
S. A. C. Hawkins ◽  
R. B. Green ◽  
I. Blamire ◽  
G. Dexter ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Bovine Spongiform Encephalopathy ◽  
Clinical Disease ◽  
Oral Challenge ◽  
Spongiform Encephalopathy

scholarly journals Erratum to: Polymorphism of the prion protein gene (PRNP) in Polish cattle affected by classical bovine spongiform encephalopathy

2012 ◽  
Vol 39 (4) ◽  
pp. 5045-5045 ◽  
Author(s):  
Artur Gurgul ◽  
Urszula Czarnik ◽  
Magdalena Larska ◽  
Mirosław P. Polak ◽  
Janusz Strychalski ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Classical Bovine Spongiform Encephalopathy
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