scholarly journals The first report of prion-related protein gene (PRNT) polymorphisms in goat

2017 ◽  
Vol 65 (2) ◽  
pp. 291-300 ◽  
Author(s):  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Gene Family ◽  
Prion Protein ◽  
Dna Sequences ◽  
Protein Gene ◽  
Prion Diseases ◽  
Genetic Research ◽  
Comparative Sequence Analysis ◽  
Prion Protein Gene ◽  
Related Protein ◽  
Prion Gene

Prion protein is encoded by the prion protein gene (PRNP). Polymorphisms of several members of the prion gene family have shown association with prion diseases in several species. Recent studies on a novel member of the prion gene family in rams have shown that prion-related protein gene (PRNT) has a linkage with codon 26 of prion-like protein (PRND). In a previous study, codon 26 polymorphism of PRND has shown connection with PRNP haplotype which is strongly associated with scrapie vulnerability. In addition, the genotype of a single nucleotide polymorphism (SNP) at codon 26 of PRND is related to fertilisation capacity. These findings necessitate studies on the SNP of PRNT gene which is connected with PRND. In goat, several polymorphism studies have been performed for PRNP, PRND, and shadow of prion protein gene (SPRN). However, polymorphism on PRNT has not been reported. Hence, the objective of this study was to determine the genotype and allelic distribution of SNPs of PRNT in 238 Korean native goats and compare PRNT DNA sequences between Korean native goats and several ruminant species. A total of five SNPs, including PRNT c.-114G > T, PRNT c.-58A > G in the upstream of PRNT gene, PRNT c.71C > T (p.Ala24Val) and PRNT c.102G > A in the open reading frame (ORF) and c.321C > T in the downstream of PRNT gene, were found in this study. All five SNPs of caprine PRNT gene in Korean native goat are in complete linkage disequilibrium (LD) with a D’ value of 1.0. Interestingly, comparative sequence analysis of the PRNT gene revealed five mismatches between DNA sequences of Korean native goats and those of goats deposited in the GenBank. Korean native black goats also showed 5 mismatches in PRNT ORF with cattle. To the best of our knowledge, this is the first genetic research of the PRNT gene in goat.

First report of prion-related protein gene (PRNT) polymorphisms in cattle

2018 ◽  
Vol 182 (25) ◽  
pp. 717-717 ◽  
Author(s):  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Gene Family ◽  
Prion Protein ◽  
Prion Diseases ◽  
Association Studies ◽  
Genetic Research ◽  
Spongiform Encephalopathy ◽  
Holstein Cattle ◽  
Related Protein ◽  
Exon 2 ◽  
Prion Gene

Prion diseases are caused by structural changes in normal prion protein (PrPC). The prion gene family includes four members: prion protein (PRNP), prion-like protein (PRND), shadow of PRNP (SPRN) and prion-related protein (PRNT). Genetic association studies of prion diseases and the other genes in the prion gene family, except for PRNT, have been performed in cattle. Our previous studies indicated that the distribution of PRNP promoter polymorphisms related with bovine spongiform encephalopathy susceptibility is significantly different in Hanwoo (Korean native cattle) and Holstein cattle. However, PRNT polymorphisms have not been reported thus far in cattle. Hence, we examined the PRNT single nucleotide polymorphisms (SNPs) in 315 Hanwoo and 140 Holstein cattle. We found a total of two SNPs, PRNT c.-87C>T and PRNT c.-37G>C, in the 5’ untranslated region of exon 2. The c.-87C>T and c.-37G>C genotype (P<0.0001) and allele (P<0.0001) frequencies exhibited significant differences in the distribution between Hanwoo and Holstein cattle. In addition, the c.-37G<C polymorphism was not found in Hanwoo. Interestingly, we did not find any polymorphisms in the ORF of bovine PRNT, which is in contrast with the highly polymorphic ovine PRNT ORF region. This is the first genetic research of the PRNT gene in cattle.

scholarly journals Identification of Prion Disease-Related Somatic Mutations in the Prion Protein Gene (PRNP) in Cancer Patients

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1480 ◽  
Author(s):  
Yong-Chan Kim ◽  
Sae-Young Won ◽  
Byung-Hoon Jeong
Keyword(s):  
Cancer Patient ◽  
Cancer Patients ◽  
Prion Protein ◽  
Patient Population ◽  
Somatic Mutations ◽  
Protein Gene ◽  
Prion Diseases ◽  
Prnp Gene ◽  
Prion Protein Gene ◽  
Total Cancer

Prion diseases are caused by misfolded prion protein (PrPSc) and are accompanied by spongiform vacuolation of brain lesions. Approximately three centuries have passed since prion diseases were first discovered around the world; however, the exact role of certain factors affecting the causative agent of prion diseases is still debatable. In recent studies, somatic mutations were assumed to be cause of several diseases. Thus, we postulated that genetically unstable cancer tissue may cause somatic mutations in the prion protein gene (PRNP), which could trigger the onset of prion diseases. To identify somatic mutations in the PRNP gene in cancer tissues, we analyzed somatic mutations in the PRNP gene in cancer patients using the Cancer Genome Atlas (TCGA) database. In addition, to evaluate whether the somatic mutations in the PRNP gene in cancer patients had a damaging effect, we performed in silico analysis using PolyPhen-2, PANTHER, PROVEAN, and AMYCO. We identified a total of 48 somatic mutations in the PRNP gene, including 8 somatic mutations that are known pathogenic mutations of prion diseases. We identified significantly different distributions among the types of cancer, the mutation counts, and the ages of diagnosis between the total cancer patient population and cancer patients carrying somatic mutations in the PRNP gene. Strikingly, although invasive breast carcinoma and glioblastoma accounted for a high percentage of the total cancer patient population (9.9% and 5.4%, respectively), somatic mutations in the PRNP gene have not been identified in these two cancer types. We suggested the possibility that somatic mutations of the PRNP gene in glioblastoma can be masked by a diagnosis of prion disease. In addition, we found four aggregation-prone somatic mutations, these being L125F, E146Q, R151C, and K204N. To the best of our knowledge, this is the first specific analysis of the somatic mutations in the PRNP gene in cancer patients.

scholarly journals Genomic Analysis and Comparison of Pakistani Camels (Camelus dromedarius) by Prion Gene

2017 ◽  
Vol 45 (1) ◽  
pp. 8
Author(s):  
Tanveer Hussain ◽  
Muneeb Musthafa ◽  
Masroor Ellahi Babar ◽  
Faiz Marikar ◽  
Fiaz Hussain ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Prion Protein ◽  
Neurodegenerative Disorders ◽  
Genomic Dna ◽  
Protein Gene ◽  
Camelus Dromedarius ◽  
Prion Protein Gene ◽  
Dromedary Camels ◽  
Prion Gene ◽  
Bactrian Camels

Background: In many parts of the Old World, domesticated camels (genus - Camelus) are an essential resource, providing food, labor, commodities, and sport to millions of people Of the three extent species, two have been domesticated (singlehumped dromedarius, Camelus dromedarius, and two humped Bactrian camels Camelus bactrianus) and one remains wild (two-humped wild Bactrian camels Camelus ferus). All three species possess a variety adaptations to harsh desert conditions, including mechanisms to tolerate of extreme temperatures, dehydration, and sandy terrain. People residing in harsh climate zones of the world are being benefitted by raising camels in terms of draft, milk, meat, hides and wool from centuries. There are different breeds of dromedary camels distributed in various parts of Pakistan; however there have been scarcity of research work on camels in Pakistan. Identification of novel link between Camel breeders with fatal neurodegenerative disorders is presence or not can be detect by a Prion gene and it was not carried out in Pakistan soil to date. Prion diseases which are a group of fatal neurodegenerative disorders affect both animals and humans. It is believed that the prions are infectious agents responsible for transmissible spongiform encephalopathies. In this study we report the first study on Prion protein gene in dromedary camels of Pakistan.Material, Methods & Results: Genes are the blueprint of life and determine the functional aspects of cellular mechanisms. Genomic DNA of the enrolled blood samples was extracted using the Nucleospin® DNA extraction kit. Genomic DNA was run on Agarose gel electrophoresis, checked the Genomic DNA quality and amplified using prion region specific primer pair. Prion protein gene was amplified (770 bp) in 35 individuals of seven dromedary camel breeds from the province Balochistan and Punjab of Pakistan. Samples having required fragment size were selected and sent for sequencing through Sanger Sequencing. All the sequences were aligned through multiple sequence alignment and edited using Codon Code aligner and explored for phylogenetic analysis. A portion of 667 bp was finally selected for phylogenetic analysis of dromedary camels from Pakistan with 61 different mammalian species (drawn from GenBank) that revealed five different clades. We found 99.9% nucleotide sequence similarities among Dromedary camels (Germany), Dromedary camels (Iran), and Dromedary camels (Pakistan). We observed deletion in dromedary camels in codon region 66-69 except wild Bactrian camels that might be the causative factor for Prion protein gene resistance in camels. The Neighbor-Joining method with bootstrap analysis of 1000 replicates was used to draw phylogenetic tree.Discussion: This study documents the presence of 14 PrP polymorphisms and shows the relationship between different camel breeds. The deletion had not previously been examined PrP allelic variation, and was found to segregate in these breeds. However, additional data are necessary to demonstrate PrP and genetic approach will be ideal for the future studies and, more investigations are necessary to demonstrate PrP genetic resistance in camels. The utility of these techniques in identifying Prion genes and selecting superior animals and culling the weak animals and making them parents of the next generation that will lead to producing more meat and milk with fewer animals are well discussed and by slaughtering of high Prion incidence will eliminate human animal fatal neurodegenerative disorders.

scholarly journals No polymorphisms in the coding region of the prion-like protein gene in Thoroughbred racehorses

2019 ◽  
Vol 67 (2) ◽  
pp. 174-182 ◽  
Author(s):  
Min-Ju Jeong ◽  
Byung-Hoon Jeong
Keyword(s):  
Amino Acid ◽  
Prion Protein ◽  
Protein Gene ◽  
Prion Diseases ◽  
Amino Acid Sequences ◽  
Prion Protein Gene ◽  
Coding Region ◽  
Thoroughbred Racehorses ◽  
Thoroughbred Horses ◽  
Protein Isoform

Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of an abnormal prion protein isoform (PrPSc), which is converted from the normal prion protein (PrPC). Prion diseases have been reported in an extensive number of species but not in horses up to now; therefore, horses are known to be a species resistant to prion diseases. The prion-like protein gene (PRND) is closely located downstream of the prion protein gene (PRNP) and the prion-like protein (Doppel) is a homologue with PrP. Previous studies have shown that an association between prion diseases and polymorphisms of the PRND gene is reported in the main hosts of prion diseases. Hence, we examined the genetic variations of the PRND gene in Thoroughbred horses. Interestingly, polymorphisms of the PRND gene were not detected. In addition, we conducted a comparative analysis of the amino acid sequences of the PRND gene to identify the differences between horses and other species. The amino acid sequence of the horse PRND gene showed the highest identity to that of sheep (83.7%), followed by that of goats, cattle and humans. To the best of our knowledge, this is the first genetic study of the PRND gene in horses.

scholarly journals Descent of the Prion Protein Gene Family from the Extracellular Domain of an Ancestral Zip Metal Ion Transporter

2010 ◽  
Vol 98 (3) ◽  
pp. 708a
Author(s):  
Holger Wille ◽  
Sepehr Ehsani ◽  
Joel C. Watts ◽  
David Westaway ◽  
Gerold Schmitt-Ulms
Keyword(s):  
Gene Family ◽  
Prion Protein ◽  
Metal Ion ◽  
Protein Gene ◽  
Extracellular Domain ◽  
Prion Protein Gene ◽  
Ion Transporter

Prion Diseases

2017 ◽  
Author(s):  
James A. Mastrianni ◽  
Joshuae G. Gallardo
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Neurodegenerative Disorders ◽  
Protein Gene ◽  
Prion Diseases ◽  
Prion Protein Gene ◽  
Secondary Transmission ◽  
Jakob Disease

Prion diseases are transmissible fatal neurodegenerative disorders resulting from the accumulation of misfolded prion protein. Although primarily sporadic diseases, 5% to 10% result from a mutation of the prion protein gene (PRNP), and less than 1% occur from exposure to prions. The current family of prion diseases includes Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker disease (GSS), fatal insomnia (FI), variant CJD (vCJD), and variably protease-sensitive prionopathy (VPSPr). Kuru is a disease of historical interest that was transmitted through cannibalistic rituals. Iatrogenic CJD (iCJD) is the result of secondary transmission of prion disease from contaminated biologicals.

scholarly journals Novel Polymorphisms and Genetic Features of the Prion Protein Gene (PRNP) in Cats, Hosts of Feline Spongiform Encephalopathy

Genes ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 13
Author(s):  
Hyeon-Ho Kim ◽  
Yong-Chan Kim ◽  
Kiwon Kim ◽  
An-Dang Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Genetic Polymorphisms ◽  
Prion Protein ◽  
Structural Stability ◽  
Prion Disease ◽  
Protein Gene ◽  
Structural Characteristics ◽  
Prion Diseases ◽  
Prnp Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene

Prion diseases are fatal neurodegenerative disorders characterized by vacuolation and gliosis in the brain. Prion diseases have been reported in several mammals, and genetic polymorphisms of the prion protein gene (PRNP) play an essential role in the vulnerability of prion diseases. However, to date, investigations of PRNP polymorphisms are rare in cats, which are the major host of feline spongiform encephalopathy (FSE). Thus, we investigated the genetic polymorphisms of the cat PRNP gene and analyzed the structural characteristics of the PrP of cats compared to those of dog, prion disease-resistant animal. To investigate the genetic variations of the cat PRNP gene in 208 cats, we performed amplicon sequencing and examined the genotype, allele and haplotype frequencies of cat PRNP polymorphisms. We evaluated the influence of cat PRNP polymorphisms using PolyPhen-2, PANTHER, PROVEAN and AMYCO. In addition, we carried out structural analysis of cat PrP according to the allele of nonsynonymous single nucleotide polymorphism (SNP) (c.457G > A, Glu153Lys) using Swiss-PdbViewer. Finally, we compared the structural differences between cat and canine PrPs for SNPs associated with prion disease resistance in dogs. We identified a total of 15 polymorphisms, including 14 novel SNPs and one insertion/deletion polymorphism (InDel). Among them, Glu153Lys was predicted to affect the structural stability and amyloid propensity of cat PrP. In addition, asparagine at codon 166 of cat PrP was predicted to have longer hydrogen bond than aspartic acid at codon 163 of canine PrP. Furthermore, substitution to dog-specific amino acids in cat PrP showed an increase in structural stability. To the best of our knowledge, this is the first study regarding the structural characteristics of cat PRNP gene.

scholarly journals Genomic assessment of the evolution of the prion protein gene family in vertebrates

Genomics ◽  
2010 ◽  
Vol 95 (5) ◽  
pp. 268-277 ◽  
Author(s):  
Paul M. Harrison ◽  
Amit Khachane ◽  
Manish Kumar
Keyword(s):  
Gene Family ◽  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene
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