Bovine spongiform encephalopathy (BSE), a member of the transmissible spongiform encepahlopathies, has been a notifiable disease in Turkey since 1997. In 2002, the BSE status of Turkey was assessed by the EU Scientific Steering Committee as "it is likely but not confirmed".This study presents the results of a targeted surveillance study to assess the presence of BSE in the age risk population of Bursa, Turkey. In the assessment procedure, the immunohistochemical detection of protease-resistant prion protein (PrP-Sc) was aimed at and applied to 420 brain tissues of cattle slaughtered in Bursa at an age of 30-months and older. None of the samples were positive for BSE.
Age Factors ; Animals ; Cattle ; Encephalopathy, Bovine Spongiform/*diagnosis/epidemiology ; Immunohistochemistry/veterinary ; Prions/*analysis ; Turkey/epidemiology

Prion diseases, including ovine scrapie, bovine spongiform encephalopathy (BSE), human kuru and Creutzfeldt-Jakob disease (CJD), originate from a conformational change of the normal cellular prion protein (PrPC) into abnormal protease-resistant prion protein (PrPSc). There is concern regarding these prion diseases because of the possibility of their zoonotic infections across species. Mutations and polymorphisms of prion sequences may influence prion-disease susceptibility through the modified expression and conformation of proteins. Rapid determination of susceptibility based on prion-sequence polymorphism information without complex structural and molecular biological analyses may be possible. Information regarding the effects of mutations and polymorphisms on prion-disease susceptibility was collected based on previous studies to classify the susceptibilities of sequences, whereas the BLOSUM62 scoring matrix and the position-specific scoring matrix were utilised to determine the distance of target sequences. The k-nearest neighbour analysis was validated with cross-validation methods. The results indicated that the number of polymorphisms did not influence prion-disease susceptibility, and three and four k-objects showed the best accuracy in identifying the susceptible group. Although sequences with negative polymorphisms showed relatively high accuracy for determination, polymorphisms may still not be an appropriate factor for estimating variation in susceptibility. Discriminant analysis of prion sequences with scoring matrices was attempted as a possible means of determining susceptibility to prion diseases. Further research is required to improve the utility of this method.
Amino Acid Sequence ; Animals ; Discriminant Analysis ; Disease Susceptibility ; Humans ; Mammals/genetics ; Mutation ; Polymorphism, Genetic ; Prion Diseases/genetics ; Prions/chemistry/genetics/*pathogenicity ; Sequence Analysis, DNA

Creutzfeldt-Jakob disease (CJD) is an uncommon neurodegenerative disorder with an incidence of 1 per 1000,000 per year typically characterized by rapidly progressive dementia, ataxia, myoclonus and behavioral changes. Genetic prion diseases, which develop due to a mutations in the prion protein gene (PRNP), account for an estimated 10 to 15% of all CJD cases. We report a 75-yr-old woman with familial CJD carrying a V180I mutation which features late onset, slow progression, no periodic sharp wave complexes on electroencephalography, and extensive cortical ribboning with spared the cerebellum and the medial occipital lobes posterior to the parieto-occipital sulcus on MRI. To our knowledge, this is the first documented case of a point mutation at codon 180 in South Korea.
Aged ; Base Sequence ; Codon ; Creutzfeldt-Jakob Syndrome/*genetics/physiopathology ; DNA Mutational Analysis ; Female ; Humans ; Neuropsychological Tests ; *Point Mutation ; Prions/*genetics ; Republic of Korea

Polymorphisms of the prion protein gene (PRNP) havebeen detected in several cervid species. In order toconfirm the genetic variations, this study examined theDNA sequences of the PRNP obtained from 33 captivesika deer (Cervus nippon laiouanus) in Korea. A total ofthree single-nucleotide polymorphisms (SNPs) at codons100, 136 and 226 in the PRNP of the sika deer wereidentified. The polymorphic site located at codon 100 hasnot been reported. The SNPs detected at codons 100 and226 induced amino acid substitutions. The SNP at codon136 was a silent mutation that does not induce any aminoacid change. The genotype and allele frequencies weredetermined for each of the SNPs.
Animals ; Base Sequence ; DNA/chemistry/genetics ; Deer/*genetics ; Genetic Variation ; Molecular Sequence Data ; Polymerase Chain Reaction/veterinary ; Polymorphism, Single Nucleotide ; Prions/*genetics ; Sequence Analysis, DNA

Prion proteins (PrPs) are infectious pathogens that cause a group of invariably fatal, neurodegenerative diseases, including Creutzfeldt-Jakob disease, by means of an entirely novel mechanism. They are produced by various species, including reptile, rodent, ruminant and mammals, during normal metabolic processes, but they can be slowly changed into pathogenic isoforms upon contact with other infectious PrP isoforms. This transmission can occur across species barriers. In the present study, phylogram for each PrP sequence was generated by PAUP* 4.0 program using Neighbor-Joining method with 1,000 times bootstrapping process for the phylogenetic analysis. The molecular dynamics (MD) simulations were performed by the SANDER module in the AMBER 7 package using Amber 99 force field. All the simulation process was conducted in the IBM p690 Supercomputing System in Korea Institute of Science and Technology Information. To reduce the calculation time, we used the Generalized Born (GB) model. We compared the sequences and structural characteristics of normal and pathogenic (E200K) human PrPs with those of other reptile, rodent, ruminant and mammalian PrPs. Phylogenetic analysis revealed that, although the turtle PrP sequence is the most distinct of the PrPs analyzed, it nonetheless retains five conserved secondary structural elements that are similar to those found in the mammalian PrPs, suggesting that these elements have important functions in vivo. The RMS deviation between the normal and E200K human PrPs was larger than that between the normal human and bovine PrPs, and all of the beta-sheet structures in human E200K PrP were very stable during MD simulations.
Animals ; Cattle ; *Computational Biology ; Humans ; Phylogeny ; Prions/*chemistry/classification/*genetics/isolation & purification ; Reptiles/metabolism ; Rodentia/metabolism ; Ruminants/metabolism ; Sequence Analysis, Protein ; Species Specificity

Since 1987, dura mater graft-associated iatrogenic Creutzfeldt-Jakob disease (dCJD) has been reported in many countries. We report the first case of dCJD in Korea. A 54-yr-old woman, who underwent resection of the meningioma in the left frontal region and received a dura mater graft 23 yr ago presented with dysesthesia followed by psychiatric symptoms and ataxia. Her neurological symptoms rapidly progressed to such an extent that she exhibited myoclonus, dementia, and pyramidal and extrapyramidal signs within 8 weeks. The 14-3-3 protein was detected in her cerebrospinal fluid; however, an electroencephalogram did not reveal characteristic positive sharp wave complexes. Diffusion-weighted magnetic resonance images, obtained serially over 64 days, revealed the rapid progression of areas of high signal intensity in the caudate nucleus and cingulate gyrus to widespread areas of high signal intensity in the cortex and basal ganglia. Pathological examination of brain biopsy specimens confirmed the presence of spongiform changes and deposition of prion protein in the neurons and neuropils.
14-3-3 Proteins/cerebrospinal fluid ; Ataxia/diagnosis ; Brain/pathology ; Creutzfeldt-Jakob Syndrome/diagnosis/pathology/*transmission ; Dementia/diagnosis ; Dura Mater/*transplantation ; Female ; Humans ; Meningioma/surgery ; Middle Aged ; Paresthesia/diagnosis ; Prions/*analysis ; Republic of Korea ; Transplants

The genetics of the prion protein gene (PRNP) play a crucial role in determining the relative susceptibility to transmissible spongiform encephalopathies (TSEs) in several mammalian species. To determine the PRNP gene variability in European red deer (Cervus elaphus), roe deer (Capreolus capreolus) and chamois (Rupicapra rupicapra), the PRNP open reading frame from 715 samples was analysed to reveal a total of ten single nucleotide polymorphisms (SNPs). In red deer, SNPs were found in codons 15, 21, 59, 78, 79, 98, 136, 168 and 226. These polymorphisms give rise to 12 haplotypes, and one of which is identical to the PRNP of American wapiti (Rocky Mountain elk, Cervus elaphus nelsoni). One silent mutation at codon 119 was detected in chamois and no SNPs were found in roe deer. This analysis confirmed that European wild ruminants have a PRNP genetic background that is compatible with TSE susceptibility, including chronic wasting disease.
Animals ; Base Sequence ; DNA/chemistry/genetics ; Deer/*genetics ; Genetic Predisposition to Disease ; Genetic Variation ; Haplotypes ; Italy ; Molecular Sequence Data ; Phylogeny ; Polymerase Chain Reaction/veterinary ; Polymorphism, Single Nucleotide ; Prion Diseases/*genetics ; Prions/*genetics ; Scotland ; Sequence Analysis, DNA