scholarly journals First Report of the Potential Bovine Spongiform Encephalopathy (BSE)-Related Somatic Mutation E211K of the Prion Protein Gene (PRNP) in Cattle

2020 ◽  
Vol 21 (12) ◽  
pp. 4246 ◽  
Author(s):  
Sae-Young Won ◽  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Somatic Mutation ◽  
Prion Disease ◽  
In Silico ◽  
Somatic Mutations ◽  
Protein Gene ◽  
Prnp Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene

Bovine spongiform encephalopathy (BSE) is a prion disease characterized by spongiform degeneration and astrocytosis in the brain. Unlike classical BSE, which is caused by prion-disease-contaminated meat and bone meal, the cause of atypical BSE has not been determined. Since previous studies have reported that the somatic mutation in the human prion protein gene (PRNP) has been linked to human prion disease, the somatic mutation of the PRNP gene was presumed to be one cause of prion disease. However, to the best of our knowledge, the somatic mutation of this gene in cattle has not been investigated to date. We investigated somatic mutations in a total of 58 samples, including peripheral blood; brain tissue including the medulla oblongata, cerebellum, cortex, and thalamus; and skin tissue in 20 individuals from each breed using pyrosequencing. In addition, we estimated the deleterious effect of the K211 somatic mutation on bovine prion protein by in silico evaluation tools, including PolyPhen-2 and PANTHER. We found a high rate of K211 somatic mutations of the bovine PRNP gene in the medulla oblongata of three Holsteins (10% ± 4.4%, 28% ± 2%, and 19.55% ± 3.1%). In addition, in silico programs showed that the K211 somatic mutation was damaging. To the best of our knowledge, this study is the first to investigate K211 somatic mutations of the bovine PRNP gene that are associated with potential BSE progression.

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 The First Report of the Prion Protein Gene (PRNP) Sequence in Pekin Ducks (Anas platyrhynchos domestica): The Potential Prion Disease Susceptibility in Ducks

Genes ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 193
Author(s):  
Min-Ju Jeong ◽  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Prion Protein ◽  
Dna Sequence ◽  
Prion Disease ◽  
Protein Gene ◽  
Prnp Gene ◽  
Pekin Duck ◽  
Prion Protein Gene ◽  
First Report ◽  
Aggregation Propensity ◽  
Pekin Ducks

Pathogenic prion protein (PrPSc), converted from normal prion protein (PrPC), causes prion disease. Although prion disease has been reported in several mammalian species, chickens are known to show strong resistance to prion diseases. In addition to chickens, the domestic duck occupies a large proportion in the poultry industry and may be regarded as a potential resistant host against prion disease. However, the DNA sequence of the prion protein gene (PRNP) has not been reported in domestic ducks. Here, we performed amplicon sequencing targeting the duck PRNP gene with the genomic DNA of Pekin ducks. In addition, we aligned the PrP sequence of the Pekin duck with that of various species using ClustalW2 and carried out phylogenetic analysis using Molecular Evolutionary Genetics Analysis X (MEGA X). We also constructed the structural modeling of the tertiary and secondary structures in avian PrP using SWISS-MODEL. Last, we investigated the aggregation propensity on Pekin duck PrP using AMYCO. We first reported the DNA sequence of the PRNP gene in Pekin ducks and found that the PrP sequence of Pekin ducks is more similar to that of geese than to that of chickens and mallards (wild ducks). Interestingly, Pekin duck PrP showed a high proportion of β-sheets compared to that of chicken PrP, and a high aggregation propensity compared to that of avian PrPs. However, Pekin duck PrP with substitutions of chicken-specific amino acids showed reduced aggregation propensities. To the best of our knowledge, this is the first report on the genetic characteristics of the PRNP sequence in Pekin ducks.

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.

Polymorphism of the prion protein gene (PRNP) in Polish cattle affected by classical bovine spongiform encephalopathy

2011 ◽  
Vol 39 (5) ◽  
pp. 5211-5217 ◽  
Author(s):  
Artur Gurgul ◽  
Czarnik Urszula ◽  
Magdalena Larska ◽  
Mirosław P. Polak ◽  
Janusz Strychalski ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Classical Bovine Spongiform Encephalopathy

scholarly journals Erratum to: Polymorphism of the prion protein gene (PRNP) in Polish cattle affected by classical bovine spongiform encephalopathy

2012 ◽  
Vol 39 (4) ◽  
pp. 5045-5045 ◽  
Author(s):  
Artur Gurgul ◽  
Urszula Czarnik ◽  
Magdalena Larska ◽  
Mirosław P. Polak ◽  
Janusz Strychalski ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Classical Bovine Spongiform Encephalopathy

Detection of Bovine Spongiform Encephalopathy-Related Prion Protein Gene Promoter Polymorphisms in Local Turkish Cattle

2008 ◽  
Vol 46 (11-12) ◽  
pp. 820-827 ◽  
Author(s):  
Cemal Ün ◽  
Kemal Oztabak ◽  
Nehir Özdemir ◽  
Dawit Tesfaye ◽  
Ahmet Mengi ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Gene ◽  
Gene Promoter ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Promoter Polymorphisms

scholarly journals Polymorphisms of the prion protein gene coding region in born-after-the-reinforced-ban (BARB) bovine spongiform encephalopathy cattle in Great Britain

2007 ◽  
Vol 88 (4) ◽  
pp. 1374-1378 ◽  
Author(s):  
G. C. Saunders ◽  
P. C. Griffiths ◽  
S. Cawthraw ◽  
A. C. Tout ◽  
P. Wiener ◽  
...  
Keyword(s):  
Great Britain ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Gene ◽  
Transmissible Spongiform Encephalopathy ◽  
Control Measures ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Coding Region ◽  
Gene Coding

Polymorphisms of the prion protein gene are associated with differing susceptibilities to transmissible spongiform encephalopathy diseases, as shown for variant Creutzfeldt–Jakob disease in humans and scrapie in sheep, but not yet in cattle. Imposition of control measures in the UK, including a reinforced ruminant feed ban in 1996, has led to a reduction in the incidence of bovine spongiform encephalopathy (BSE). BSE-affected cattle born after 1996 in Great Britain have been termed born-after-the-reinforced-ban (BARB) cases. In this study, the PrP gene coding region from 100 BARB BSE cases and 66 matched healthy-control cattle was sequenced to investigate whether this would reveal a genetic basis to their origin. Polymorphisms identified were not found to be associated with increased susceptibility to BSE in the BARB cases. Analysis of BARB cases grouped either by clinical status or by whether they formed an isolated or clustered case was also undertaken, but differences were not found to be significant.

Additions and corrections: Prion protein gene sequence of Canada's first non-imported case of bovine spongiform encephalopathy (BSE)

Genome ◽  
2004 ◽  
Vol 47 (1) ◽  
pp. 229-229
Author(s):  
Michael B Coulthart ◽  
Rhonda Mogk ◽  
Jason M Rancourt ◽  
Deborah L Godal ◽  
Stefanie Czub
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Gene Sequence ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Imported Case
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