scholarly journals Analysis of the PRNP gene polymorphisms in healthy Greek sheep during 2012 – 2016

2018 ◽  
Vol 69 (1) ◽  
pp. 839
Author(s):  
E. BOUKOUVALA ◽  
E. KATHAROPOULOS ◽  
S. CHRISTOFORIDOU ◽  
M. BABETSA ◽  
L. V. EKATERINIADOU
Keyword(s):  
Genetic Resistance ◽  
Prnp Gene ◽  
Classical Scrapie ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Breeding Programs ◽  
Spongiform Encephalopathies ◽  
Blood Samples ◽  
Taqman Probes ◽  
The Central Nervous System

Scrapie is a slowly progressive infectious disease of sheep and goats that causes degeneration of the central nervous system. Scrapie is one of several transmissible spongiform encephalopathies (TSEs), like the bovine spongiform encephalopathy (BSE). In sheep, polymorphisms at codons 136, 154 and 171 of the host gene PRPN that encodes the PrP protein, are known to be closely linked to susceptibility or resistance to natural and experimental classical scrapie. In many countries, but not in Greece, breeding programs have been implemented to increase genetic resistance. This study was supported mainly by the private initiatives of farmers willing to improve their flocks by increasing the resistance to scrapie. Thus, the PrP genotypes (of the three mentioned codons) from 5815 blood samples of clinically healthy rams from 160 healthy flocks during the period 2012 – 2016 were determined. Additionally, 1399 blood samples were genotyped only for the 171 codon. Samples were analyzed by Real Time PCR (TaqMan probes) with specific labeled probes. Our results showed an increased percentage of the two genotypes, ARR/ARR and ARR/ARQ linked with resistance to the disease (27.29% and 34.6%, respectively) and relatively reduced percentage of the genotype ARQ/ARQ (24.23%) which is associated with susceptibility to disease and is the most common genotype in the Greek flocks. This joined effort has resulted in the establishment of an important number of farms with an increased population of genetically resistant rams to classical scrapie.

scholarly journals Scrapie Resistance Gene Identification using Optimized Taqman Test qPCR Method in Sheep on the Territory of the Republic of Serbia

2021 ◽  
Vol 71 (2) ◽  
pp. 189-197
Author(s):  
Slađan Nešić ◽  
Stefan Jelisić ◽  
Sanja Aleksić-Kovačević ◽  
Milan Aničić ◽  
Ivana Vučićević
Keyword(s):  
Gene Identification ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathies ◽  
Resistant Genotype ◽  
Taqman Probes ◽  
Qpcr Method ◽  
The Central Nervous System ◽  
Polymerase Chain ◽  
The Republic ◽  
Prp Gene

Abstract Scrapie is an infectious neurodegenerative disease affecting the central nervous system of sheep and goats that belongs to transmissible spongiform encephalopathies. The disease is caused by the accumulation of proteinase-resistant isoform of the prion protein. The sheep predisposition to scrapie is associated with polymorphisms of the PrP gene. Genetic susceptibility to scrapie is mainly related to codons 136, 154, and 171. ARR sheep are strongly scrapie resistant and VRQ genotype is the most susceptible. Many countries have scrapie eradication programs based on using rams with resistant genotype. The eradication program has not yet been implemented in the Republic of Serbia. To examine the genetic makeup of sheep in Serbia related to scrapie, we optimized TaqMan probes of real-time polymerase chain reaction (qPCR) technique for three codons. Blood samples from 100 sheep were analyzed by qPCR and the majority of the examined sheep were AA homozygous for the 136 codon. For codon 154 the most frequent genotype was RR and for codon 171 the most frequent genotype was QQ.

scholarly journals Prion protein genetics: Host PrP control of TSE susceptibility

2005 ◽  
Vol 27 (4) ◽  
pp. 20-23
Author(s):  
Wilfred Goldmann
Keyword(s):  
Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Spongiform Encephalopathies ◽  
Degenerative Disorders ◽  
Jakob Disease ◽  
The Central Nervous System ◽  
Important Host ◽  
Disease Family ◽  
Sheep Scrapie

TSEs (transmissible spongiform encephalopathies) are fatal, degenerative disorders of the central nervous system. The best-known members of this disease family are sheep scrapie, cattle BSE (bovine spongiform encephalopathy) and human CJD (Creutzfeldt–Jakob disease). By far the most important host gene in TSEs is the PrP (prion protein) gene. It modulates TSE susceptibility at many levels and is the crucial element in the treatment and eradication of these diseases. This article will highlight the advances in our understanding of PrP genetics in animals and man.

scholarly journals Prion Strain- and Species-Dependent Effects of Antiprion Molecules in Primary Neuronal Cultures

2007 ◽  
Vol 81 (24) ◽  
pp. 13794-13800 ◽  
Author(s):  
Sabrina Cronier ◽  
Vincent Beringue ◽  
Anne Bellon ◽  
Jean-Michel Peyrin ◽  
Hubert Laude
Keyword(s):  
Transmissible Spongiform Encephalopathy ◽  
Cell System ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Neuronal Cultures ◽  
Primary Neuronal Cultures ◽  
Spongiform Encephalopathies ◽  
The Central Nervous System

ABSTRACT Transmissible spongiform encephalopathies (TSE) arise as a consequence of infection of the central nervous system by prions and are incurable. To date, most antiprion compounds identified by in vitro screening failed to exhibit therapeutic activity in animals, thus calling for new assays that could more accurately predict their in vivo potency. Primary nerve cell cultures are routinely used to assess neurotoxicity of chemical compounds. Here, we report that prion strains from different species can propagate in primary neuronal cultures derived from transgenic mouse lines overexpressing ovine, murine, hamster, or human prion protein. Using this newly developed cell system, the activity of three generic compounds known to cure prion-infected cell lines was evaluated. We show that the antiprion activity observed in neuronal cultures is species or strain dependent and recapitulates to some extent the activity reported in vivo in rodent models. Therefore, infected primary neuronal cultures may be a relevant system in which to investigate the efficacy and mode of action of antiprion drugs, including toward human transmissible spongiform encephalopathy agents.

scholarly journals Demographic risk factors for classical and atypical scrapie in Great Britain

2007 ◽  
Vol 88 (12) ◽  
pp. 3486-3492 ◽  
Author(s):  
Darren M. Green ◽  
Victor J. del Rio Vilas ◽  
Colin P. D. Birch ◽  
Jethro Johnson ◽  
Istvan Z. Kiss ◽  
...  
Keyword(s):  
European Union ◽  
Great Britain ◽  
Classical Scrapie ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Atypical Scrapie ◽  
The European Union ◽  
Spongiform Encephalopathies ◽  
Breeding Programmes ◽  
Trading Network

Following the bovine spongiform encephalopathy (BSE) crisis, the European Union has introduced policies for eradicating transmissible spongiform encephalopathies (TSEs), including scrapie, from large ruminants. However, recent European Union surveillance has identified a novel prion disease, ‘atypical’ scrapie, substantially different from classical scrapie. It is unknown whether atypical scrapie is naturally transmissible or zoonotic, like BSE. Furthermore, cases have occurred in scrapie-resistant genotypes that are targets for selection in legislated selective breeding programmes. Here, the first epidemiological study of British cases of atypical scrapie is described, focusing on the demographics and trading patterns of farms and using databases of recorded livestock movements. Triplet comparisons found that farms with atypical scrapie stock more sheep than those of the general, non-affected population. They also move larger numbers of animals than control farms, but similar numbers to farms reporting classical scrapie. Whilst there is weak evidence of association through sheep trading of farms reporting classical scrapie, atypical scrapie shows no such evidence, being well-distributed across regions of Great Britain and through the sheep-trading network. Thus, although cases are few in number so far, our study suggests that, should natural transmission of atypical scrapie be occurring at all, it is doing so slowly.

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.

How to Limit the Spread of Creutzfeldt-Jakob Disease

1996 ◽  
Vol 17 (8) ◽  
pp. 521-528
Author(s):  
Dominique Dormont
Keyword(s):  
Blood Donation ◽  
Transmissible Spongiform Encephalopathy ◽  
Infected Individual ◽  
Experimental Models ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Spongiform Encephalopathies ◽  
Corneal Grafting ◽  
Jakob Disease ◽  
Spleen And Lymph Nodes

AbstractTransmissible spongiform encephalopathies are rare lethal diseases induced in humans and animals by unconventional agents called transmissible spongiform encephalopathy agents (TSEAs), virions, or prions. Several cases of iatrogenic Creutzfeldt-Jakob disease (CJD) have been reported in the literature after neuro-surgery, treatment with pituitary-derived hormones, corneal grafting, and use of dura mater lyophilisates. In a given infected individual, TSEA-associated infectiousness depends on the nature of the organ: the central nervous system has the highest infectiousness, spleen and lymph nodes a medium infectiousness, and organs such as bone, skin, or skeletal muscles do not harbor any detectable infectiousness in experimental models. Transmissible spongiform encephalopathy/prions have unconventional properties; in particular, they resist almost all the chemical and physical processes that inactivate conventional viruses. Therefore, prevention of CJD agent transmission must be taken into account in daily hospital practice. Efficient sterilization procedures should be determined. In tissue and blood donation, donors with a neurologic history must be excluded, and patients treated with pituitary-derived hormones should be considered potentially infected with TSEA and excluded.

scholarly journals A case–control study of scrapie Nor98 in Norwegian sheep flocks

2006 ◽  
Vol 87 (12) ◽  
pp. 3729-3736 ◽  
Author(s):  
Petter Hopp ◽  
Mohamed K. Omer ◽  
Berit T. Heier
Keyword(s):  
Prion Protein ◽  
Case Control Study ◽  
Demographic Data ◽  
Case Control ◽  
Classical Scrapie ◽  
Transmissible Spongiform Encephalopathies ◽  
Indirect Contact ◽  
Spongiform Encephalopathies ◽  
Animal Contact ◽  
Control Study

Scrapie is a fatal, neurological disease of sheep and goats and belongs to the transmissible spongiform encephalopathies. In 1998, a new type of scrapie, designated scrapie Nor98, was detected in Norway. Scrapie Nor98 differs from classical scrapie in the distribution of pathological changes and of the scrapie prion protein, the Western blot profile of the prion protein, and with isolated cases usually being observed in the case flocks. In 2004, a case–control study was conducted on scrapie Nor98 with 28 cases and 102 randomly selected controls. The questionnaire included questions on demographic data, animal contact between sheep flocks, indirect contact with equipment, use of concentrate feed and supplemental feeds, and use of medicines and vaccines. The data were analysed by using logistic regression with the sheep flock as the statistical unit. In the final model, the detection of scrapie Nor98 was related to the practice of not removing all afterbirths, the use of vitamin and mineral feed supplements, the absence of concentrate feed of swine or poultry on the farm and the presence of dogs on the farm. The results show that the epidemiology of scrapie Nor98 differs from that of classical scrapie in that no risk factors that indicate transmission of scrapie Nor98 between flocks by movement or direct contact between animals were found. Furthermore, the association between scrapie Nor98 and mineral intake shown herein should be explored further. Although the possibility that scrapie Nor98 has a low transmissibility between animals under natural conditions cannot be ruled out, the results would also be in accordance with a spontaneous aetiology.

scholarly journals Sympathetic Prions

2001 ◽  
Vol 1 ◽  
pp. 555-556 ◽  
Author(s):  
Markus Glatzel
Keyword(s):  
Gastrointestinal Tract ◽  
Injection Site ◽  
Peripheral Nerves ◽  
Infectious Agent ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Membrane Glycoprotein ◽  
Spongiform Encephalopathies ◽  
Jakob Disease ◽  
The Brain

Transmissible spongiform encephalopathies are a group of invariably fatal neurodegenerative diseases. The infectious agent is termed prion and is thought to be composed of a modified protein (PrPSc or PrPRES), a protease-resistant conformer of the normal host-encoded membrane glycoprotein, PrPC[1]. Bovine spongiform encephalopathy, scrapie of sheep, and Creutzfeldt-Jakob disease are among the most notable transmissible spongiform encephalopathies. Prions are most efficiently propagated trough intracerebral inoculation, yet the entry point of the infectious agent is often through peripheral sites like the gastrointestinal tract[2,3]. The process by which prions invade the brain is termed neuroinvasion[4]. We and others have speculated that, depending on the amount of infectious agent injected, the injection site, and the strain of prions employed, neuroinvasion can occur either directly via peripheral nerves or first through the lymphoreticular system and then via peripheral nerves[5].

scholarly journals Classical BSE prions emerge from asymptomatic pigs challenged with atypical/Nor98 scrapie

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Belén Marín ◽  
Alicia Otero ◽  
Séverine Lugan ◽  
Juan Carlos Espinosa ◽  
Alba Marín-Moreno ◽  
...  
Keyword(s):  
Protein Misfolding ◽  
Clinical Signs ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Post Inoculation ◽  
Atypical Scrapie ◽  
Wasting Disease ◽  
Spongiform Encephalopathies ◽  
Robust Transmission

AbstractPigs are susceptible to infection with the classical bovine spongiform encephalopathy (C-BSE) agent following experimental inoculation, and PrPSc accumulation was detected in porcine tissues after the inoculation of certain scrapie and chronic wasting disease isolates. However, a robust transmission barrier has been described in this species and, although they were exposed to C-BSE agent in many European countries, no cases of natural transmissible spongiform encephalopathies (TSE) infections have been reported in pigs. Transmission of atypical scrapie to bovinized mice resulted in the emergence of C-BSE prions. Here, we conducted a study to determine if pigs are susceptible to atypical scrapie. To this end, 12, 8–9-month-old minipigs were intracerebrally inoculated with two atypical scrapie sources. Animals were euthanized between 22- and 72-months post inoculation without clinical signs of TSE. All pigs tested negative for PrPSc accumulation by enzyme immunoassay, immunohistochemistry, western blotting and bioassay in porcine PrP mice. Surprisingly, in vitro protein misfolding cyclic amplification demonstrated the presence of C-BSE prions in different brain areas from seven pigs inoculated with both atypical scrapie isolates. Our results suggest that pigs exposed to atypical scrapie prions could become a reservoir for C-BSE and corroborate that C-BSE prions emerge during interspecies passage of atypical scrapie.

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