Genotype distribution of the prion protein gene (PRNP) promoter polymorphisms in Korean cattle

Genome ◽  
2006 ◽  
Vol 49 (12) ◽  
pp. 1539-1544 ◽  
Author(s):  
Byung-Hoon Jeong ◽  
Yun-Jung Lee ◽  
Nam-Ho Kim ◽  
R.I. Carp ◽  
Yong-Sun Kim
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Holstein Cattle ◽  
Genotype Distribution ◽  
Prion Protein Gene ◽  
Indel Polymorphism ◽  
Promoter Polymorphisms ◽  
Hanwoo Cattle ◽  
German Cattle

Recently, an association between bovine spongiform encephalopathy (BSE) and insertion/deletion (indel) polymorphisms in the bovine prion protein gene (PRNP) promoter region has been reported in German cattle. These PRNP polymorphisms cause changes in PRNP expression and are thought to play an important role in BSE susceptibility. BSE has been reported in British and Japanese Holstein cattle but has not been diagnosed in Hanwoo cattle (Bos taurus coreanae) up to now. These results prompted us to investigate the genotype distributions of these PRNP promoter polymorphisms in 107 Hanwoo cattle and 52 Holstein cattle and compare the results with those of previous studies. A significant difference (P = 0.0249) in allele frequency of the 23 bp indel polymorphism was observed between Hanwoo and the BSE-affected German cattle previously investigated. There were no significant differences in the genotype (P = 0.2095) or allele (P = 0.8875) frequencies of the 12 bp indel polymorphism between Hanwoo and BSE-affected German cattle. Interestingly, the genotype and allele frequencies of the 23 bp indel polymorphism in Korean Holsteins were very similar to those previously reported for BSE-affected German cattle and healthy US cattle sires.

Bovine spongiform encephalopathy (BSE) associated polymorphisms of the prion-like protein gene (PRND) in Korean dairy cattle and Hanwoo

2018 ◽  
Vol 85 (1) ◽  
pp. 7-11 ◽  
Author(s):  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Dairy Cattle ◽  
Bovine Spongiform Encephalopathy ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Holstein Cattle ◽  
Genotype Distribution ◽  
Korean Cattle ◽  
Significant Difference ◽  
Hanwoo Cattle ◽  
German Cattle

Bovine spongiform encephalopathy (BSE) involves insertion/deletion (in/del) polymorphisms in the prion protein gene (PRNP) promoter region that are associated with vulnerability to disease progression. Recently, a second member of the prion gene family, prion-like protein gene (PRND), has been reported to show the PRND R132Q polymorphism, which is associated with the susceptibility to BSE in German Fleckvieh breeds. The objective of this study was to examine the genotype, allele, and haplotype frequencies of PRND gene in Korean cattle and evaluate their susceptibility to BSE. We did this in 277 Korean native cattle (Hanwoo) and 124 Korean dairy cattle (Holstein) by direct sequencing and compared the R132Q genotype frequency between BSE-affected German cattle and Korean cattle. The results indicated a total of 5 single nucleotide polymorphisms (SNPs) including PRND c.149G > A (p.50Arg > His; R50H), PRND c.285C > T (C4819T), PRND c.395G > A (p.132Arg > Gln; R132Q) and PRND c.528T > A (T5063A) in the open reading frame (ORF) and c.602C > G in the 3′ untranslated region (UTR) of exon 2 in Korean Holstein and Hanwoo cattle. Except for c.149G > A, the remaining 4 SNPs showed significantly different genotype and allele frequencies between the Korean Holstein and Hanwoo (P < 0·01). There were no significant differences in genotype distribution of c.395G > A SNP between BSE-affected German and Korean Holstein cattle (P = 0·6778), but a significant difference was detected between BSE-affected German cattle and Hanwoo cattle (P = 0·0028). The results suggest that Hanwoo cattle may possess a relatively more BSE-resistant genotype than Korean Holstein cattle.

scholarly journals Scrapie susceptibility-associated indel polymorphism of shadow of prion protein gene (SPRN) in Korean native black goats

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Yong-Chan Kim ◽  
Seon-Kwan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Allele Frequencies ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Indel Polymorphism ◽  
Spongiform Encephalopathies ◽  
Direct Dna Sequencing ◽  
Significant Difference

Abstract Prion diseases in sheep and goats are called scrapie and belong to a group of transmissible spongiform encephalopathies (TSEs) caused by the abnormal misfolding of the prion protein encoded by the prion protein gene (PRNP). The shadow of the prion protein gene (SPRN) is the only prion gene family member that shows a protein expression profile similar to that of the PRNP gene in the central nervous system. In addition, genetic susceptibility of the SPRN gene has been reported in variant Creutzfeldt–Jakob disease (CJD), bovine spongiform encephalopathy (BSE) and scrapie. However, genetic studies of the SPRN gene have not been carried out in Korean native black goats. Here, we investigated the genotype and allele frequencies of SPRN polymorphisms in 213 Korean native black goats and compared these polymorphisms with those previously reported for scrapie-affected animals. We found a total of 6 polymorphisms including 1 nonsynonymous single nucleotide polymorphism (SNP) and 1 synonymous SNP in the open reading frame (ORF) region and 3 SNPs and 1 indel polymorphism (c.495_496insCTCCC) in the 3′ untranslated region (UTR) by direct DNA sequencing. A significant difference in the allele frequency of the c.495_496insCTCCC indel polymorphism was found between the Italian scrapie-affected goats and the Korean native black goats (P < 0.001). Furthermore, there was a significant difference in the allele frequencies of the c.495_496insCTCCC indel polymorphism between Italian healthy goats and Korean native black goats (P < 0.001). To evaluate the biological impact of the novel nonsynonymous SNP c.416G > A (Arg139Gln), we carried out PROVEAN analysis. PROVEAN predicted the SNP as ‘Neutral’ with a score of −0.297. To the best of our knowledge, this is the first genetic study of the SPRN gene in Korean native black goats.

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 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.

Spongiform encephalopathy in siblings with no evidence of protease-resistant prion protein or a mutation in the prion protein gene

2013 ◽  
Vol 260 (7) ◽  
pp. 1871-1879 ◽  
Author(s):  
Daniela Varges ◽  
Walter J. Schulz-Schaeffer ◽  
Wiebke M. Wemheuer ◽  
Insa Damman ◽  
Matthias Schmitz ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene

Analysis of sequence variability of the bovine prion protein gene ( PRNP ) in German cattle breeds

Neurogenetics ◽  
2004 ◽  
Vol 5 (1) ◽  
pp. 19-25 ◽  
Author(s):  
Petra Sander ◽  
Henning Hamann ◽  
Ina Pfeiffer ◽  
Wilhelm Wemheuer ◽  
Bertram Brenig ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
Sequence Variability ◽  
Cattle Breeds ◽  
German Cattle

300 HEMIZYGOUS PRION PROTEIN GENE (PRNP) KNOCKOUT IN CATTLE FIBROBLASTS

2008 ◽  
Vol 20 (1) ◽  
pp. 230
Author(s):  
D. Brunetti ◽  
G. Rossi ◽  
I. Lagutina ◽  
R. Duchi ◽  
S. Colleoni ◽  
...  
Keyword(s):  
Southern Blot ◽  
Prion Protein ◽  
Cell Lines ◽  
Protein Gene ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Drug Resistant ◽  
Bovine Strain ◽  
Fetal Fibroblasts ◽  
Adult Fibroblasts

Bovine spongiform encephalopathy (BSE) represents a real threat for human health, as has been demonstrated by the causal link with the variant form of Creutzfeldt-Jakob disease. The aim of our project is to create a bovine strain knockout for the prion protein gene (PRNP) that should be resistant to BSE infection. We combined the use of homologous recombination by PRNP targeting vectors in bovine fibroblasts with the subsequent use of nuclear transfer (NT). We transfected fetal (male) and adult (female) bovine fibroblasts by nucleofection, using targeting vectors disrupting the PRNP by means of loxP flanked cassettes. They expressed resistance to different drugs driven by a PGK or TK promoter and the thymidine kinase gene as a negative selection marker. We screened, by PCR, 907 drug-resistant colonies, from which we identified 8 Neo-resistant colonies with a recombined PRNP allele (overall efficiency 3.2%; 7/108 from fetal, 1/145 from adult; P < 0.5). Fibroblasts PRNP+/– Neo were used to produce NT blastocysts from which neural precursors cell lines were established (Lazzari et al. 2006 Stem Cells 24, 2514–2521). These lines were capable of extensive proliferation (over 120 doublings during 4 months of culture) and provided unlimited material for Southern blot analysis to confirm PCR findings. Three clones (2 from fetal and 1 from adult) were further analyzed and confirmed PRNP+/– by Southern blot and were subsequently used for NT to generate blastocysts for transfer to recipient heifers. On Day +40 of gestation, the pregnancy rate was 33.3% (9/30) for the fetal line and 50% (2/4) for the adult line. One of the fetuses originating from fetal fibroblasts was removed on Day +45 to establish a rejuvenated fibroblast cell line used for a second round of gene targeting to obtain a PRNP –/– clone. We nucleofected these fibroblasts with Puro, Hygro, and promoterless Hygro cassette-carrying targeting vectors. We screened 625 drug-resistant colonies by PCR but none tested positive for the second targeting. In conclusion, we have obtained heterozygous PRNP+/– fibroblasts with the Neo vector both in fetal and adult fibroblasts, but failed with other vectors. In the first targeting, the efficiency was 10 times greater in fetal v. adult fibroblasts. The derivation of neural precursor cell lines from cloned blastocysts is a useful procedure to have sufficient material for molecular analysis without the need of rejuvenating the cell through the production of a fetus. None of the vectors used for the targeting of the second allele was successful.

scholarly journals Codon 129 polymorphism of prion protein gene in is not a risk factor for Alzheimer's disease

2013 ◽  
Vol 71 (7) ◽  
pp. 423-427 ◽  
Author(s):  
Jerusa Smid ◽  
Michele Christine Landemberger ◽  
Valéria Santoro Bahia ◽  
Vilma Regina Martins ◽  
Ricardo Nitrini
Keyword(s):  
Risk Factor ◽  
Cognitive Performance ◽  
Prion Protein ◽  
Protein Gene ◽  
Apoe Genotype ◽  
Genotype Distribution ◽  
Prion Protein Gene ◽  
Apolipoprotein E Gene ◽  
Jakob Disease ◽  
Codon 129

Interaction of prion protein and amyloid-b oligomers has been demonstrated recently. Homozygosity at prion protein gene (PRNP) codon 129 is associated with higher risk for Creutzfeldt-Jakob disease. This polymorphism has been addressed as a possible risk factor in Alzheimer disease (AD).ObjectiveTo describe the association between codon 129 polymorphisms and AD.MethodsWe investigated the association of codon 129 polymorphism of PRNP in 99 AD patients and 111 controls, and the association between this polymorphism and cognitive performance. Other polymorphisms of PRNP and additive effect of apolipoprotein E gene (ApoE) were evaluated.ResultsCodon 129 genotype distribution in AD 45.5% methionine (MM), 42.2% methionine valine (MV), 12.1% valine (VV); and 39.6% MM, 50.5% MV, 9.9% VV among controls (p>0.05). There were no differences of cognitive performance concerning codon 129. Stratification according to ApoE genotype did not reveal difference between groups.ConclusionCodon 129 polymorphism is not a risk factor for AD in Brazilian patients.

scholarly journals Prion Protein Gene (PRNP) Sequences Suggest Differing Vulnerability to Chronic Wasting Disease for Florida Key Deer (Odocoileus virginianus clavium) and Columbian White-Tailed Deer (O. v. leucurus)

2020 ◽  
Vol 111 (6) ◽  
pp. 564-572
Author(s):  
Tolulope I N Perrin-Stowe ◽  
Yasuko Ishida ◽  
Emily E Terrill ◽  
Brian C Hamlin ◽  
Linda Penfold ◽  
...  
Keyword(s):  
Odocoileus Virginianus ◽  
Prion Protein ◽  
Protein Gene ◽  
Chronic Wasting Disease ◽  
Synonymous Substitution ◽  
Spongiform Encephalopathy ◽  
Prion Protein Gene ◽  
Wasting Disease ◽  
Genetic Vulnerability ◽  
Key Deer

Abstract Chronic wasting disease (CWD) is a fatal, highly transmissible spongiform encephalopathy caused by an infectious prion protein. CWD is spreading across North American cervids. Studies of the prion protein gene (PRNP) in white-tailed deer (WTD; Odocoileus virginianus) have identified non-synonymous substitutions associated with reduced CWD frequency. Because CWD is spreading rapidly geographically, it may impact cervids of conservation concern. Here, we examined the genetic vulnerability to CWD of 2 subspecies of WTD: the endangered Florida Key deer (O. v. clavium) and the threatened Columbian WTD (O. v. leucurus). In Key deer (n = 48), we identified 3 haplotypes formed by 5 polymorphisms, of which 2 were non-synonymous. The polymorphism c.574G&gt;A, unique to Key deer (29 of 96 chromosomes), encodes a non-synonymous substitution from valine to isoleucine at codon 192. In 91 of 96 chromosomes, Key deer carried c.286G&gt;A (G96S), previously associated with substantially reduced susceptibility to CWD. Key deer may be less genetically susceptible to CWD than many mainland WTD populations. In Columbian WTD (n = 13), 2 haplotypes separated by one synonymous substitution (c.438C&gt;T) were identified. All of the Columbian WTD carried alleles that in other mainland populations are associated with relatively high susceptibility to CWD. While larger sampling is needed, future management plans should consider that Columbian WTD are likely to be genetically more vulnerable to CWD than many other WTD populations. Finally, we suggest that genetic vulnerability to CWD be assessed by sequencing PRNP across other endangered cervids, both wild and in captive breeding facilities.

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