scholarly journals Classical Bovine Spongiform Encephalopathy by Transmission of H-Type Prion in Homologous Prion Protein Context

2011 ◽  
Vol 17 (9) ◽  
pp. 1636-1644 ◽  
Author(s):  
Juan-María Torres
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Spongiform Encephalopathy ◽  
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

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

scholarly journals Presence of subclinical infection in gene-targeted human prion protein transgenic mice exposed to atypical bovine spongiform encephalopathy

2013 ◽  
Vol 94 (12) ◽  
pp. 2819-2827 ◽  
Author(s):  
Rona Wilson ◽  
Karen Dobie ◽  
Nora Hunter ◽  
Cristina Casalone ◽  
Thierry Baron ◽  
...  
Keyword(s):  
Human Health ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Disease Transmission ◽  
Large Scale ◽  
Single Agent ◽  
Diagnostic Methods ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Human Prion Protein

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.

scholarly journals Discriminating Scrapie and Bovine Spongiform Encephalopathy Isolates by Infrared Spectroscopy of Pathological Prion Protein

2004 ◽  
Vol 279 (32) ◽  
pp. 33847-33854 ◽  
Author(s):  
Achim Thomzig ◽  
Sashko Spassov ◽  
Manuela Friedrich ◽  
Dieter Naumann ◽  
Michael Beekes
Keyword(s):  
Infrared Spectroscopy ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Spongiform Encephalopathy

scholarly journals Prevalent abnormal prion protein in human appendixes after bovine spongiform encephalopathy epizootic: large scale survey

BMJ ◽  
2013 ◽  
Vol 347 (oct15 5) ◽  
pp. f5675-f5675 ◽  
Author(s):  
O. N. Gill ◽  
Y. Spencer ◽  
A. Richard-Loendt ◽  
C. Kelly ◽  
R. Dabaghian ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Large Scale ◽  
Spongiform Encephalopathy ◽  
Large Scale Survey

scholarly journals First Report of the Potential Bovine Spongiform Encephalopathy (BSE)-Related Somatic Mutation E211K of the Prion Protein Gene (PRNP) in Cattle

2020 ◽  
Vol 21 (12) ◽  
pp. 4246 ◽  
Author(s):  
Sae-Young Won ◽  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Somatic Mutation ◽  
Prion Disease ◽  
In Silico ◽  
Somatic Mutations ◽  
Protein Gene ◽  
Prnp Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene

Bovine spongiform encephalopathy (BSE) is a prion disease characterized by spongiform degeneration and astrocytosis in the brain. Unlike classical BSE, which is caused by prion-disease-contaminated meat and bone meal, the cause of atypical BSE has not been determined. Since previous studies have reported that the somatic mutation in the human prion protein gene (PRNP) has been linked to human prion disease, the somatic mutation of the PRNP gene was presumed to be one cause of prion disease. However, to the best of our knowledge, the somatic mutation of this gene in cattle has not been investigated to date. We investigated somatic mutations in a total of 58 samples, including peripheral blood; brain tissue including the medulla oblongata, cerebellum, cortex, and thalamus; and skin tissue in 20 individuals from each breed using pyrosequencing. In addition, we estimated the deleterious effect of the K211 somatic mutation on bovine prion protein by in silico evaluation tools, including PolyPhen-2 and PANTHER. We found a high rate of K211 somatic mutations of the bovine PRNP gene in the medulla oblongata of three Holsteins (10% ± 4.4%, 28% ± 2%, and 19.55% ± 3.1%). In addition, in silico programs showed that the K211 somatic mutation was damaging. To the best of our knowledge, this study is the first to investigate K211 somatic mutations of the bovine PRNP gene that are associated with potential BSE progression.

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