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 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.

Role of the PrP Gene in Transmissible Spongiform Encephalopathies

Intervirology ◽  
1993 ◽  
Vol 35 (1-4) ◽  
pp. 164-175 ◽  
Author(s):  
Charles Weissmann ◽  
Hansruedi Büeler ◽  
Marek Fischer ◽  
Michel Aguet
Keyword(s):  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathies ◽  
Prp Gene

scholarly journals Prion propagation in a nerve conduit model containing segments devoid of axons

2007 ◽  
Vol 88 (12) ◽  
pp. 3479-3485 ◽  
Author(s):  
Christine Kratzel ◽  
Dominique Krüger ◽  
Michael Beekes
Keyword(s):  
Molecular Mechanisms ◽  
Transport Processes ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathies ◽  
Nerve Conduits ◽  
Sciatic Neurectomy ◽  
Prion Propagation ◽  
Causative Agents ◽  
The Central Nervous System ◽  
Cellular Components

Prions, the putative causative agents of transmissible spongiform encephalopathies, are neurotropic pathogens that spread to the central nervous system via synaptically linked neural conduits upon peripheral infection. Axons and their transport processes have been suggested as mediators of nerve-associated prion dissemination. However, the exact cellular components and molecular mechanisms underlying neural spread are unknown. This study used an established hamster scrapie model to pursue a novel experimental approach using nerve conduits containing segments devoid of neurites generated by incomplete nerve regeneration following Wallerian degeneration to probe the necessity of axons for the neural propagation of prions. For this purpose, animals were subjected to unilateral sciatic neurectomy 4 weeks before footpad inoculation with scrapie agent. The results showed that the regional nerve is the prime conduit for cerebral neuroinvasion and revealed, as evidenced by the accumulation of pathological prion protein PrPTSE, that prions can proceed along segments of peripheral neural projections without detectable axonal structures.

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 Targeted knock-down of cellular prion protein expression in myelinating Schwann cells does not alter mouse prion pathogenesis

2013 ◽  
Vol 94 (6) ◽  
pp. 1435-1440 ◽  
Author(s):  
Sophie Halliez ◽  
Nathalie Chesnais ◽  
Giovanna Mallucci ◽  
Marthe Vilotte ◽  
Christelle Langevin ◽  
...  
Keyword(s):  
Nervous System ◽  
Schwann Cells ◽  
Prion Protein ◽  
Cellular Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathies ◽  
The Central Nervous System ◽  
Myelinated Nerves ◽  
Pathogenic Agents ◽  
The Brain

In naturally acquired transmissible spongiform encephalopathies, the pathogenic agents or prions spread from the sites of initial peripheral uptake or replication to the brain where they cause progressive and fatal neurodegeneration. Routing via the peripheral nervous system is considered to be one of the main pathways to the central nervous system. Replication of prions in Schwann cells is viewed as a potentially important mechanism for efficient prion spread along nerves. Here we used a Cre-loxP mouse transgenetic approach to disrupt host-encoded prion protein (PrPC) specifically in myelinating Schwann cells. Despite the use of infection routes targeting highly myelinated nerves, there was no alteration in mouse prion pathogenesis, suggesting that conversion-dependent, centripetal spread of prions does not crucially rely on PrPC expressed by myelinating Schwann cells.

scholarly journals Ovine prion protein variant A136R154L168Q171 increases resistance to experimental challenge with bovine spongiform encephalopathy agent

2006 ◽  
Vol 87 (12) ◽  
pp. 3741-3745 ◽  
Author(s):  
Wilfred Goldmann ◽  
Fiona Houston ◽  
Paula Stewart ◽  
Matteo Perucchini ◽  
James Foster ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Protein Variant ◽  
Spongiform Encephalopathies ◽  
The Standard Model ◽  
Incubation Periods ◽  
Prp Gene ◽  
Bovine Spongiform Encephalopathy Agent ◽  
Experimental Challenge

Susceptibility and incubation periods of transmissible spongiform encephalopathies, such as scrapie in sheep, are modulated by the PrP gene. The standard model of association between ovine PrP genetics and classical scrapie susceptibility is based on PrP genotypes with respect to codons 136, 154 and 171, e.g. alanine–arginine–glutamine (ARQ). It is demonstrated here that a proline to leucine substitution in codon 168 of the ovine PrP protein gene is associated with increased resistance to experimental bovine spongiform encephalopathy (BSE) inoculation. The ARL168Q PrP allele was found in heterozygous ARP168Q/ARL168Q sheep that have so far survived intravenous BSE challenge three times longer than BSE-challenged homozygous ARP168Q/ARP168Q sheep, which develop disease in around 700 days. In contrast, the L141F polymorphism does not appear to be associated with susceptibility to intravenous BSE challenge.

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 Experimental inoculation of CD11c+ B1 lymphocytes, CD68+ macrophages, or platelet-rich plasma from scrapie-infected sheep into susceptible sheep results in variable infectivity

2020 ◽  
Vol 2 (9) ◽  
Author(s):  
Najiba Mammadova ◽  
Eric D. Cassmann ◽  
S. Jo Moore ◽  
Eric M. Nicholson ◽  
Justin J. Greenlee
Keyword(s):  
Disease Transmission ◽  
Platelet Rich Plasma ◽  
White Blood Cells ◽  
Transmissible Spongiform Encephalopathies ◽  
Blood Components ◽  
Spongiform Encephalopathies ◽  
Prion Infection ◽  
Prion Infectivity ◽  
Jakob Disease ◽  
The Central Nervous System

Many studies have demonstrated prion infectivity in whole blood and blood components in a variety of transmissible spongiform encephalopathies of livestock and rodents, and variant Creutzfeldt–Jakob disease in humans, as well as an association between pathogenic prion protein (PrPSc) and different immune cells (e.g. follicular dendritic cells, T and B lymphocytes, monocytes and tingible body macrophages). To further investigate the role of various blood components in prion disease transmission, we intracranially inoculated genetically susceptible VRQ/ARQ and ARQ/ARQ sheep with inocula composed of CD11c+ B1 lymphocytes, CD68 +macrophages, or platelet-rich plasma derived from clinically ill sheep infected with the US no. 13–7 scrapie agent. At the completion of the study, we found that VRQ/ARQ and ARQ/ARQ sheep inoculated with CD11c+ B1 lymphocytes and CD68+ macrophages developed scrapie with detectable levels of PrPSc in the central nervous system and lymphoreticular system, while those inoculated with platelet-rich plasma did not develop disease and did not have detectable PrPSc by immunohistochemistry or enzyme immunoassay. This study complements and expands on earlier findings that white blood cells harbour prion infectivity, and reports CD11c+ B1 lymphocytes and CD68+ macrophages as additional targets for possible preclinical detection of prion infection in blood.

scholarly journals Molecular Detection of Cellular Prion Protein in Brain Tissues of Black Bengal Goats in Bangladesh

2015 ◽  
Vol 3 (2) ◽  
pp. 1-4
Author(s):  
Nasrin Sultana ◽  
Mohd Zahirul Islam Khan ◽  
Emdadul Haque Choudhury ◽  
Md Rafiqul Islam
Keyword(s):  
Prion Protein ◽  
Molecular Detection ◽  
Cellular Prion Protein ◽  
The Central Nervous System ◽  
Membrane Bound ◽  
Polymerase Chain ◽  
First Time ◽  
The Brain ◽  
Prp Gene ◽  
Brain Tissues

The cellular prion protein (PrPC) is a membrane-bound glycoprotein mainlypresent in the central nervous system which is necessary for the establishmentand further evolution of prion disease in human and animals. The aim of thepresent study was to investigate the PrPC protein in brain tissues of black Bengalgoat. Fifteen brain tissues were collected from different slaughter houses ofthree districts (Mymensingh, Manikgonj and Netrokona) of Bangladesh duringJanuary to February, 2011. The PrPC protein was detected in the brain tissuesof black Bengal goats using polymerase chain reaction. The result showed allpositive (100%) of the amplified samples. The standardized PCR could be usedfor detection of PrPC protein in different tissues of animals and humans.Sequencing of PrP gene in the black Bengal goats for the risk assessment ofscrapie is needed for further study. To our knowledge, detection of PrPC proteinin the brain tissues of indigenous goats is the first time in Bangladesh.

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