scholarly journals Prion protein gene polymorphisms in healthy and scrapie-affected Spanish sheep

2004 ◽  
Vol 85 (7) ◽  
pp. 2103-2110 ◽  
Author(s):  
Cristina Acín ◽  
Inmaculada Martín-Burriel ◽  
Wilfred Goldmann ◽  
Jaber Lyahyai ◽  
Marta Monzón ◽  
...  
Keyword(s):  
Amino Acid ◽  
Prion Protein ◽  
Protein Gene ◽  
Haplotype Frequency ◽  
The Novel ◽  
Low Frequencies ◽  
Reading Frame ◽  
Healthy Sheep ◽  
Gene Open Reading Frame ◽  
Prp Gene

The Rasa Aragonesa sheep is the second most important Spanish breed after the Merino breed. Reported here is the prion protein (PrP) haplotype frequency distribution for scrapie-related codons (136, 154 and 171) and a sequencing study of the complete PrP gene open reading frame for this breed and six other closely related breeds. The study includes four scrapie-affected sheep flocks belonging to Rasa Aragonesa and Rasa Navarra breeds. Thirty-eight scrapie-affected sheep, 502 healthy sheep from scrapie-affected flocks and 905 sheep from a breed survey were genotyped. The most frequent PrP haplotype in both scrapie and healthy flocks was ARQ, which was found at significantly higher frequency in scrapie-affected sheep. The susceptibility-associated VRQ haplotype was found at low frequencies in six out of eight breeds, but was not present in the 38 scrapie-affected sheep. The resistance-associated ARR haplotype was found in all breeds except one (Ojinegra) at frequencies ⩾14 %. Fourteen amino acid polymorphisms were detected in these Spanish sheep, including the known amino acid substitutions at codons 112, 136, 141, 143, 154, 171 and 176, and new polymorphisms at codons 101 (Q→R), 151 (R→G), 151 (R→H), 172 (Y→D) and 175 (Q→E). Most of the novel polymorphic codons show frequencies lower than 5 %.

scholarly journals Prion protein gene polymorphisms in healthy and scrapie-affected sheep in Greece

2004 ◽  
Vol 85 (2) ◽  
pp. 547-554 ◽  
Author(s):  
Charalambos Billinis ◽  
Vassilios Psychas ◽  
Leonidas Leontides ◽  
Vassiliki Spyrou ◽  
Stamatis Argyroudis ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Denaturing Gradient Gel Electrophoresis ◽  
Gradient Gel Electrophoresis ◽  
Healthy Control ◽  
The Moment ◽  
Chios Sheep ◽  
Prp Gene ◽  
Control Study ◽  
Clinical Cases

A total of 216 local crossbred sheep from 16 scrapie-affected Greek flocks and 210 purebred sheep of the milk breeds Chios and Karagouniko from healthy flocks were analysed for scrapie-linked polymorphisms in the prion protein (PrP) gene. Of the 216 sheep in this case–control study, 96 sheep were clinical cases, 25 subclinical cases (asymptomatic at the moment of euthanasia but positive by histopathology and/or ELISA detecting proteinase-resistant PrP) and 95 healthy controls (negative by all evaluations). Polymorphisms at codons 136, 154 and 171 were determined by denaturing gradient gel electrophoresis, followed by RFLP and sequencing. Scrapie, both clinical and subclinical, was associated with the genotypes ARQ/ARQ (88 of 110 sheep of that genotype), ARQ/TRQ (9 of 13), ARQ/AHQ (15 of 38) and VRQ/VRQ (9 of 17). Histopathological lesions were more severe in the clinical cases. Genotypes ARQ/ARR (26 sheep), ARQ/ARK (seven sheep), AHQ/ARR (one sheep), ARH/ARH (one sheep) and ARR/ARH (three sheep) were detected exclusively in healthy control sheep. In the purebred survey, four genotypes were present in the Chios sheep (ARQ/ARQ, ARQ/TRQ, ARQ/AHQ and ARQ/ARR) and four in the Karagouniko sheep (ARQ/ARQ, ARQ/AHQ, ARQ/ARR and ARQ/ARH).

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.

Glycine cleavage enzyme complex: Rabbit H-protein cDNA sequence analysis and comparison to human, cow, and chicken

2000 ◽  
Vol 78 (6) ◽  
pp. 725-730 ◽  
Author(s):  
Francis Choy ◽  
Lisa Sharp ◽  
Derek A Applegarth
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Matrix Protein ◽  
Protein Gene ◽  
Mitochondrial Targeting ◽  
Reading Frame ◽  
Cleavage Enzyme ◽  
Glycine Cleavage ◽  
H Protein ◽  
Sequence Similarities

The H-protein is one of the four essential components (H-, L-, P-, and T-proteins) of the mammalian glycine cleavage enzyme complex, the major degradative pathway of glycine. We have isolated the full-length cDNA of the H-protein gene from the rabbit (Oryctolagus caniculus) by reverse transcription of liver poly-A mRNA and determined its nucleotide sequence (GenBank Acc. No. BankIt 318281 AF 231451). Similar to that in human, the rabbit H-protein gene possesses a 519-bp open reading frame that translates a 173-amino-acid (aa) protein. This reading frame is comprised of a 48-aa mitochondrial targeting sequence and a 125-aa residue that constitutes the mature mitochondrial matrix protein. In the mature protein region, there is a 95.5% nucleotide and 98.4% amino-acid sequence similarity to human. This conservation was also noted in the mature protein of the cow (Bos taurus) and chicken (Gallus domesticus), where there are a 94.1% and 85.3% nucleotide similarities, and 95.2% and 85.6% amino-acid sequence similarities, respectively. However, the targeting region is not as well conserved. Comparison of the rabbit targeting sequence to that in human, cow, and chicken reveals 84.0%, 79.2%, and 72.9% nucleotide, and 72.9%, 75.0%, and 54.2% amino-acid sequence similarities, respectively. These findings suggest that within the H-protein gene, the regions encoding the mitochondrial targeting and matrix protein may have evolved differently. Gene diversification in the former may reflect the species specificity in targeting proteins destined for the mitochondria, whereas homology in the latter suggests a very similar structure-function of the mature H-protein among these species. This homology in structure-function likely accounts for the observation that non-human H-protein can replace the human protein in the activity assay of the glycine cleavage enzyme system. This includes the biochemical diagnosis of non-ketotic hyperglycinemia (NKH) resulting from defects other than the H-protein, e.g., mutation(s) in the P-protein.Key words: glycine cleavage enzyme, H-protein, sequence comparison, non-ketotic hyperglycinemia.

scholarly journals The First Report of Genetic Polymorphisms of the Equine SPRN Gene in Outbred Horses, Jeju and Halla Horses

Animals ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 2574
Author(s):  
Sae-Young Won ◽  
Yong-Chan Kim ◽  
Kyoungtag Do ◽  
Byung-Hoon Jeong
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Protein Gene ◽  
Prion Diseases ◽  
Minimum Free Energy ◽  
Nucleotide Polymorphisms ◽  
Single Nucleotide ◽  
Reading Frame ◽  
Direct Dna Sequencing ◽  
Thoroughbred Horses

Prion disease is a fatal infectious disease caused by the accumulation of pathogenic prion protein (PrPSc) in several mammals. However, to date, prion disease has not been reported in horses. The Sho protein encoded by the shadow of the prion protein gene (SPRN) plays an essential role in the pathomechanism of prion diseases. To date, the only genetic study of the equine SPRN gene has been reported in the inbred horse, Thoroughbred horse. We first discovered four SPRN single nucleotide polymorphisms (SNPs) in 141 Jeju and 88 Halla horses by direct DNA sequencing. In addition, we found that the genotype, allele and haplotype frequencies of these SNPs of Jeju horses were significantly different from those of Halla and Thoroughbred horses, this latter breed is also included in this study. Furthermore, we observed that the minimum free energy and mRNA secondary structure were significantly different according to haplotypes of equine SPRN polymorphisms by the RNAsnp program. Finally, we compared the SNPs in the coding sequence (CDS) of the SPRN gene between horses and prion disease-susceptible species. Notably, prion disease-susceptible animals had polymorphisms that cause amino acid changes in the open reading frame (ORF) of the SPRN gene, while these polymorphisms were not found in horses.

ESTIMATING CAUSALITY OF THE NOVEL PRION PROTEIN GENE VARIANT T201S

2016 ◽  
Vol 87 (12) ◽  
pp. e1.136-e1
Author(s):  
Tze How Mok ◽  
Carolin Koriath ◽  
Tracy Campbell ◽  
Romi Saha ◽  
Thomas Clement Truelsen ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
The Novel ◽  
Gene Variant

scholarly journals Efficient Transmission of Two Different Sheep Scrapie Isolates in Transgenic Mice Expressing the Ovine PrP Gene

2001 ◽  
Vol 75 (11) ◽  
pp. 5328-5334 ◽  
Author(s):  
Carole Crozet ◽  
Frederic Flamant ◽  
Anna Bencsik ◽  
Denise Aubert ◽  
Jacques Samarut ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Prion Protein ◽  
Neuron Specific Enolase ◽  
Open Reading Frame ◽  
Protein Accumulation ◽  
Spongiform Encephalopathies ◽  
Reading Frame ◽  
Neurological Signs ◽  
Prp Gene ◽  
Sheep Scrapie

ABSTRACT We produced transgenic mice expressing the sheep prion protein to obtain a sensitive model for sheep spongiform encephalopathies (scrapie). The complete open reading frame, with alanine, arginine, and glutamine at susceptibility codons 136, 154, and 171, respectively, was inserted downstream from the neuron-specific enolase promoter. A mouse line, Tg(OvPrP4), devoid of the murine PrP gene, was obtained by crossing with PrP knockout mice. Tg(OvPrP4) mice were shown to selectively express sheep PrP in their brains, as demonstrated in mRNA and protein analysis. We showed that these mice were susceptible to infection by sheep scrapie following intracerebral inoculation with two natural sheep scrapie isolates, as demonstrated not only by the occurrence of neurological signs but also by the presence of the spongiform changes and abnormal prion protein accumulation in their brains. Mean times to death of 238 and 290 days were observed with these isolates, but the clinical course of the disease was strikingly different in the two cases. One isolate led to a very early onset of neurological signs which could last for prolonged periods before death. Independently of the incubation periods, some of the mice inoculated with this isolate showed low or undetectable levels of PrPsc, as detected by both Western blotting and immunohistochemistry. The development of experimental scrapie in these mice following inoculation of the scrapie infectious agent further confirms that neuronal expression of the PrP open reading frame alone is sufficient to mediate susceptibility to spongiform encephalopathies. More importantly, these mice provide a new and promising tool for studying the infectious agents in sheep spongiform encephalopathies.

scholarly journals Absence of single nucleotide polymorphisms (SNPs) in the open reading frame (ORF) of the prion protein gene (PRNP) in a large sampling of various chicken breeds

BMC Genomics ◽  
2019 ◽  
Vol 20 (1) ◽  
Author(s):  
Yong-Chan Kim ◽  
Sae-Young Won ◽  
Byung-Hoon Jeong
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Protein Gene ◽  
Open Reading Frame ◽  
High Dose ◽  
Prion Protein Gene ◽  
Genetic Characteristics ◽  
Reading Frame ◽  
Disease Resistant ◽  
Chicken Breeds

Abstract Background Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP). Currently, although several prion disease-resistant animals have been reported, a high dose of prion agent inoculation triggers prion disease infection in these disease-resistant animals. However, in chickens, natural prion disease-infected cases have not been reported, and experimental challenges with prion agents have failed to cause infection. Unlike other prion disease-resistant animals, chickens have shown perfect resistance to prion disease thus far. Thus, investigation of the chicken PRNP gene could improve for understanding the mechanism of perfect prion-disease resistance. Here, we investigated the genetic characteristics of the open reading frame (ORF) of the chicken PRNP gene in a large sampling of various chicken breeds. Results We found only tandem repeat deletion polymorphisms of the chicken PRNP ORF in the 4 chicken breeds including 106 Dekalb White, 100 Ross, 98 Ogolgye and 100 Korean native chickens. In addition, the distribution of chicken insertion/deletion polymorphisms was significantly different among the 4 chicken breeds. Finally, we found significant differences in the number of PRNP SNPs between prion disease-susceptible species and prion disease-resistant species. Notably, chickens lack SNPs in the ORF of the prion protein. Conclusion In this study, we found that the absence of SNPs in the chicken PRNP ORF is a notable feature of animals with perfect resistant to prion disease.

scholarly journals Genetic Variation in the Prion Protein Gene (PRNP) of Two Tunisian Goat Populations

Animals ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 1635
Author(s):  
Samia Kdidi ◽  
Mohamed Habib Yahyaoui ◽  
Michela Conte ◽  
Barbara Chiappini ◽  
Mohamed Hammadi ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Transmissible Spongiform Encephalopathies ◽  
Prion Protein Gene ◽  
Breeding Programs ◽  
Low Frequencies ◽  
Spongiform Encephalopathies ◽  
Prolonged Incubation ◽  
Global View ◽  
First Time

Scrapie is a fatal prion disease. It belongs to transmissible spongiform encephalopathies (TSEs), and occurs in sheep and goats. Similarly, to ovine species, the prion protein gene (PRNP) plays a major role in conferring resistance or susceptibility to TSE in goats. This study assesses the variability of PRNP in native and crossed-breed goat populations raised in the Southeast of Tunisia and provides information on the distribution of PRNP haplotypes and genotypes in these goat populations. A total of 116 unrelated goats including 82 native and 34 crossed-breed goats were screened for PRNP polymorphisms using Sanger sequencing. Sequence analysis revealed 10 non-synonymous polymorphisms (G37V, M137I, R139S, I142M, H143R, N146D, R154H, R211Q, Q222K, and S240P), giving rise to 12 haplotypes and 23 genotypes. Moreover, four silent mutations were detected at codons 30, 42, 138, and 179; the former was reported for the first time in goat (nucleotide 60 c→t). Interestingly, the PrP variants associated with resistance (D146 and K222) or with a prolonged incubation time of goat to scrapie (M142, R143, H154, Q211) were absent or detected with low frequencies except for H154 variant, which is present with high frequency (1%, 1%, 4%, 0%, 88%, and 6%, respectively, for native goats, and 0%, 1%, 0%, 1%, 78%, and 1%, respectively, for crossed goats). The analysis of PRNP polymorphisms of goats raised in other regions of the country will be useful in getting a global view of PRNP genetic variability and the feasibility of goat breeding programs in Tunisia.

A novel 17β-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: new insights into the evolution of steroid-hormone signalling

1999 ◽  
Vol 337 (3) ◽  
pp. 425-431 ◽  
Author(s):  
Tea LANIŠNIK RIŽNER ◽  
Gabriele MOELLER ◽  
Hubert H. THOLE ◽  
Marija ŽAKELJ-MAVRIČ ◽  
Jerzy ADAMSKI
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Magnaporthe Grisea ◽  
Hydroxysteroid Dehydrogenase ◽  
Cdna Clones ◽  
The Novel ◽  
Reading Frame ◽  
Cochliobolus Lunatus ◽  
Acid Protein ◽  
History Of

17β-Hydroxysteroid dehydrogenase (17β-HSD) from the filamentous fungus Cochliobolus lunatus (17β-HSDcl) catalyses the reduction of steroids and of several o- and p-quinones. After purification of the enzyme, its partial amino acid sequence was determined. A PCR fragment amplified with primers derived from peptide sequences was generated for screening the Coch. lunatus cDNA library. Three independent full-length cDNA clones were isolated and sequenced, revealing an 810-bp open reading frame encoding a 270-amino-acid protein. After expression in Escherichia coli and purification to homogeneity, the enzyme was found to be active towards androstenedione and menadione, and was able to form dimers of Mr 60000. The amino acid sequence of the novel 17β-HSD demonstrated high homology with fungal carbonyl reductases, such as versicolorin reductase from Emericella nidulans (Aspergillus nidulans; VerA) and Asp. parasiticus (Ver1), polyhydroxynaphthalene reductase from Magnaporthe grisea, the product of the Brn1 gene from Coch. heterostrophus and a reductase from Colletotrichum lagenarium, which are all members of the short-chain dehydrogenase/reductase superfamily. 17β-HSDcl is the first discovered fungal 17β-hydroxysteroid dehydrogenase belonging to this family. The primary structure of this enzyme may therefore help to elucidate the evolutionary history of steroid dehydrogenases.

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