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.

scholarly journals Review: Update on Classical and Atypical Scrapie in Sheep and Goats

2018 ◽  
Vol 56 (1) ◽  
pp. 6-16 ◽  
Author(s):  
Justin J. Greenlee
Keyword(s):  
Prion Protein ◽  
Environmental Contamination ◽  
Protein Misfolding ◽  
Transmissible Spongiform Encephalopathy ◽  
Classical Scrapie ◽  
Spongiform Encephalopathy ◽  
Atypical Scrapie ◽  
Sheep And Goats ◽  
Scrapie Agent ◽  
Scrapie Strains

Scrapie is a naturally occurring transmissible spongiform encephalopathy (TSE) or prion disease of sheep and goats. Scrapie is a protein misfolding disease where the normal prion protein (PrPC) misfolds into a pathogenic form (PrPSc) that is highly resistant to enzymatic breakdown within the cell and accumulates, eventually leading to neurodegeneration. The amino acid sequence of the prion protein and tissue distribution of PrPSc within affected hosts have a major role in determining susceptibility to and potential environmental contamination with the scrapie agent. Many countries have genotype-based eradication programs that emphasize using rams that express arginine at codon 171 in the prion protein, which is associated with resistance to the classical scrapie agent. In classical scrapie, accumulation of PrPSc within lymphoid and other tissues facilitates environmental contamination and spread of the disease within flocks. A major distinction can be made between classical scrapie strains that are readily spread within populations of susceptible sheep and goats and atypical (Nor-98) scrapie that has unique molecular and phenotype characteristics and is thought to occur spontaneously in older sheep or goats. This review provides an overview of classical and atypical scrapie with consideration of potential transmission of classical scrapie to other mammalian hosts.

scholarly journals Reduced susceptibility to bovine spongiform encephalopathy prions in transgenic mice expressing a bovine PrP with five octapeptide repeats

2007 ◽  
Vol 88 (6) ◽  
pp. 1842-1849 ◽  
Author(s):  
Alejandro Brun ◽  
Alfonso Gutiérrez-Adán ◽  
Joaquín Castilla ◽  
Belén Pintado ◽  
Fayna Díaz-San Segundo ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
De Novo ◽  
Natural Source ◽  
Proteinase K ◽  
Spongiform Encephalopathy ◽  
Intracerebral Inoculation ◽  
Prion Infection ◽  
Cattle Breeds

In this work, transgenic (Tg) mice were generated expressing a bovine prion protein containing five octarepeats (BoPrP5OR-Tg). After intracerebral inoculation of bovine spongiform encephalopathy (BSE) inoculum, these mice suffered a BSE-like neuropathology but survived longer compared with homologous Tg mice expressing similar levels of a six octarepeat BoPrP protein (BoPrP6OR-Tg). De novo-generated five octarepeat (5OR) PrPSc showed no biochemical differences from 6OR-PrPSc, and the proteinase K-resistant core (PrPres) was biochemically indistinguishable from the 6OR counterpart. Lower susceptibility to BSE is suggested for BoPrP5OR-Tg mice, as they were not as efficient at replicating BSE prions from the same natural source inoculum as BoPrP6OR-Tg mice expressing similar PrPC levels. These results raise the possibility of selecting cattle breeds bearing the 5OR Prnp allele that are less susceptible to prion infection.

scholarly journals Prion Protein Alleles Showing a Protective Effect on the Susceptibility of Sheep to Scrapie and Bovine Spongiform Encephalopathy

2007 ◽  
Vol 81 (13) ◽  
pp. 7306-7309 ◽  
Author(s):  
Gabriele Vaccari ◽  
Claudia D'Agostino ◽  
Romolo Nonno ◽  
Francesca Rosone ◽  
Michela Conte ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protective Effect ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Amino Acid Substitution ◽  
Classical Scrapie ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Spongiform Encephalopathies ◽  
Disease Eradication

ABSTRACT The susceptibility of sheep to classical scrapie and bovine spongiform encephalopathy (BSE) is mainly influenced by prion protein (PrP) polymorphisms A136V, R154H, and Q171R, with the ARR allele associated with significantly decreased susceptibility. Here we report the protective effect of the amino acid substitution M137T, I142K, or N176K on the ARQ allele in sheep experimentally challenged with either scrapie or BSE. Such observations suggest the existence of additional PrP alleles that significantly decrease the susceptibility of sheep to transmissible spongiform encephalopathies, which may have important implications for disease eradication strategies.

Sign in / Sign up

Export Citation Format

Share Document