scholarly journals Bovine Spongiform Encephalopathy Agent in a Prion Protein (PrP)ARR/ARRGenotype Sheep after Peripheral Challenge: Complete Immunohistochemical Analysis of Disease‐Associated PrP and Transmission Studies to Ovine‐Transgenic Mice

2007 ◽  
Vol 195 (7) ◽  
pp. 989-996 ◽  
Author(s):  
Anna Bencsik ◽  
Thierry Baron
Keyword(s):  
Transgenic Mice ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Immunohistochemical Analysis ◽  
Spongiform Encephalopathy ◽  
Transmission Studies ◽  
Bovine Spongiform Encephalopathy Agent

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.

scholarly journals Enhanced Virulence of Sheep-Passaged Bovine Spongiform Encephalopathy Agent Is Revealed by Decreased Polymorphism Barriers in Prion Protein Conversion Studies

2013 ◽  
Vol 88 (5) ◽  
pp. 2903-2912 ◽  
Author(s):  
J. Priem ◽  
J. P. M. Langeveld ◽  
L. J. M. van Keulen ◽  
F. G. van Zijderveld ◽  
O. Andreoletti ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Spongiform Encephalopathy ◽  
Bovine Spongiform Encephalopathy Agent

scholarly journals Transgenic Mice Expressing Porcine Prion Protein Resistant to Classical Scrapie but Susceptible to Sheep Bovine Spongiform Encephalopathy and Atypical Scrapie

2009 ◽  
Vol 15 (8) ◽  
pp. 1214-1221 ◽  
Author(s):  
Juan-Carlos Espinosa ◽  
María-Eugenia Herva ◽  
Olivier Andréoletti ◽  
Danielle Padilla ◽  
Caroline Lacroux ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Classical Scrapie ◽  
Spongiform Encephalopathy ◽  
Atypical Scrapie ◽  
Protein Resistant

scholarly journals Assessing the Susceptibility of Transgenic Mice Overexpressing Deer Prion Protein to Bovine Spongiform Encephalopathy

2013 ◽  
Vol 88 (3) ◽  
pp. 1830-1833 ◽  
Author(s):  
C. M. Vickery ◽  
R. Lockey ◽  
T. M. Holder ◽  
L. Thorne ◽  
K. E. Beck ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Spongiform Encephalopathy

scholarly journals Molecular Analysis of the Protease-Resistant Prion Protein in Scrapie and Bovine Spongiform Encephalopathy Transmitted to Ovine Transgenic and Wild-Type Mice

2004 ◽  
Vol 78 (12) ◽  
pp. 6243-6251 ◽  
Author(s):  
Thierry Baron ◽  
Carole Crozet ◽  
Anne-Gaëlle Biacabe ◽  
Sandrine Philippe ◽  
Jérémie Verchere ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Transmissible Spongiform Encephalopathy ◽  
Spongiform Encephalopathy ◽  
Infectious Agents ◽  
Wild Type ◽  
Molecular Features ◽  
Different Strains ◽  
Scrapie Strains

ABSTRACT The existence of different strains of infectious agents involved in scrapie, a transmissible spongiform encephalopathy (TSE) of sheep and goats, remains poorly explained. These strains can, however, be differentiated by characteristics of the disease in mice and also by the molecular features of the protease-resistant prion protein (PrPres) that accumulates into the infected tissues. For further analysis, we first transmitted the disease from brain samples of TSE-infected sheep to ovine transgenic [Tg(OvPrP4)] and to wild-type (C57BL/6) mice. We show that, as in sheep, molecular differences of PrPres detected by Western blotting can differentiate, in both ovine transgenic and wild-type mice, infection by the bovine spongiform encephalopathy (BSE) agent from most scrapie sources. Similarities of an experimental scrapie isolate (CH1641) with BSE were also likewise found following transmission in ovine transgenic mice. Secondly, we transmitted the disease to ovine transgenic mice by inoculation of brain samples of wild-type mice infected with different experimental scrapie strains (C506M3, 87V, 79A, and Chandler) or with BSE. Features of these strains in ovine transgenic mice were reminiscent of those previously described for wild-type mice, by both ratios and by molecular masses of the different PrPres glycoforms. Moreover, these studies revealed the diversity of scrapie strains and their differences with BSE according to labeling by a monoclonal antibody (P4). These data, in an experimental model expressing the prion protein of the host of natural scrapie, further suggest a genuine diversity of TSE infectious agents and emphasize its linkage to the molecular features of the abnormal prion protein.

Sign in / Sign up

Export Citation Format

Share Document