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  1 / 3152 MEDLINE  
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[PMID]:29422098
[Au] Autor:Huyben D; Boqvist S; Passoth V; Renström L; Allard Bengtsson U; Andréoletti O; Kiessling A; Lundh T; Vågsholm I
[Ad] Endereço:Department of Animal Nutrition and Management, Swedish University of Agricultural Sciences, 75007, Uppsala, Sweden. david.huyben@slu.se.
[Ti] Título:Screening of intact yeasts and cell extracts to reduce Scrapie prions during biotransformation of food waste.
[So] Source:Acta Vet Scand;60(1):9, 2018 Feb 08.
[Is] ISSN:1751-0147
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Yeasts can be used to convert organic food wastes to protein-rich animal feed in order to recapture nutrients. However, the reuse of animal-derived waste poses a risk for the transmission of infectious prions that can cause neurodegeneration and fatality in humans and animals. The aim of this study was to investigate the ability of yeasts to reduce prion activity during the biotransformation of waste substrates-thereby becoming a biosafety hurdle in such a circular food system. During pre-screening, 30 yeast isolates were spiked with Classical Scrapie prions and incubated for 72 h in casein substrate, as a waste substitute. Based on reduced Scrapie seeding activity, waste biotransformation and protease activities, intact cells and cell extracts of 10 yeasts were further tested. Prion analysis showed that five yeast species reduced Scrapie seeding activity by approximately 1 log10 or 90%. Cryptococcus laurentii showed the most potential to reduce prion activity since both intact and extracted cells reduced Scrapie by 1 log10 and achieved the highest protease activity. These results show that select forms of yeast can act as a prion hurdle during the biotransformation of waste. However, the limited ability of yeasts to reduce prion activity warrants caution as a sole barrier to transmission as higher log reductions are needed before using waste-cultured yeast in circular food systems.
[Mh] Termos MeSH primário: Biotransformação
Príons/metabolismo
Scrapie/prevenção & controle
Gerenciamento de Resíduos/métodos
Leveduras/metabolismo
[Mh] Termos MeSH secundário: Animais
Extratos Celulares/análise
Alimentos
Parasitologia de Alimentos/normas
Parasitologia de Alimentos/tendências
Peptídeo Hidrolases/metabolismo
Gerenciamento de Resíduos/normas
Leveduras/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Extracts); 0 (Prions); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180210
[St] Status:MEDLINE
[do] DOI:10.1186/s13028-018-0363-y


  2 / 3152 MEDLINE  
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[PMID]:29220360
[Au] Autor:Eigenbrod S; Frick P; Bertsch U; Mitteregger-Kretzschmar G; Mielke J; Maringer M; Piening N; Hepp A; Daude N; Windl O; Levin J; Giese A; Sakthivelu V; Tatzelt J; Kretzschmar H; Westaway D
[Ad] Endereço:Center for Neuropathology and Prion Research, Ludwig Maximilians University, Munich, Germany.
[Ti] Título:Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.
[So] Source:PLoS One;12(12):e0188989, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prion diseases have been linked to impaired copper homeostasis and copper induced-oxidative damage to the brain. Divalent metal ions, such as Cu2+ and Zn2+, bind to cellular prion protein (PrPC) at octapeptide repeat (OR) and non-OR sites within the N-terminal half of the protein but information on the impact of such binding on conversion to the misfolded isoform often derives from studies using either OR and non-OR peptides or bacterially-expressed recombinant PrP. Here we created new transgenic mouse lines expressing PrP with disrupted copper binding sites within all four histidine-containing OR's (sites 1-4, H60G, H68G, H76G, H84G, "TetraH>G" allele) or at site 5 (composed of residues His-95 and His-110; "H95G" allele) and monitored the formation of misfolded PrP in vivo. Novel transgenic mice expressing PrP(TetraH>G) at levels comparable to wild-type (wt) controls were susceptible to mouse-adapted scrapie strain RML but showed significantly prolonged incubation times. In contrast, amino acid replacement at residue 95 accelerated disease progression in corresponding PrP(H95G) mice. Neuropathological lesions in terminally ill transgenic mice were similar to scrapie-infected wt controls, but less severe. The pattern of PrPSc deposition, however, was not synaptic as seen in wt animals, but instead dense globular plaque-like accumulations of PrPSc in TgPrP(TetraH>G) mice and diffuse PrPSc deposition in (TgPrP(H95G) mice), were observed throughout all brain sections. We conclude that OR and site 5 histidine substitutions have divergent phenotypic impacts and that cis interactions between the OR region and the site 5 region modulate pathogenic outcomes by affecting the PrP globular domain.
[Mh] Termos MeSH primário: Histidina/química
Proteínas Priônicas/química
Scrapie/patologia
[Mh] Termos MeSH secundário: Animais
Camundongos
Camundongos Transgênicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prion Proteins); 4QD397987E (Histidine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188989


  3 / 3152 MEDLINE  
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[PMID]:28910420
[Au] Autor:Groveman BR; Raymond GJ; Campbell KJ; Race B; Raymond LD; Hughson AG; Orrú CD; Kraus A; Phillips K; Caughey B
[Ad] Endereço:Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, United States of America.
[Ti] Título:Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.
[So] Source:PLoS Pathog;13(9):e1006623, 2017 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian prion structures and replication mechanisms are poorly understood. Most synthetic recombinant prion protein (rPrP) amyloids prepared without cofactors are non-infectious or much less infectious than bona fide tissue-derived PrPSc. This effect has been associated with differences in folding of the aggregates, manifested in part by reduced solvent exclusion and protease-resistance in rPrP amyloids, especially within residues ~90-160. Substitution of 4 lysines within residues 101-110 of rPrP (central lysine cluster) with alanines (K4A) or asparagines (K4N) allows formation of aggregates with extended proteinase K (PK) resistant cores reminiscent of PrPSc, particularly when seeded with PrPSc. Here we have compared the infectivity of rPrP aggregates made with K4N, K4A or wild-type (WT) rPrP, after seeding with scrapie brain homogenate (ScBH) or normal brain homogenate (NBH). None of these preparations caused clinical disease on first passage into rodents. However, the ScBH-seeded fibrils (only) led to a subclinical pathogenesis as indicated by increases in prion seeding activity, neuropathology, and abnormal PrP in the brain. Seeding activities usually accumulated to much higher levels in animals inoculated with ScBH-seeded fibrils made with the K4N, rather than WT, rPrP molecules. Brain homogenates from subclinical animals induced clinical disease on second passage into "hamsterized" Tg7 mice, with shorter incubation times in animals inoculated with ScBH-seeded K4N rPrP fibrils. On second passage from animals inoculated with ScBH-seeded WT fibrils, we detected an additional PK resistant PrP fragment that was similar to that of bona fide PrPSc. Together these data indicate that both the central lysine cluster and scrapie seeding of rPrP aggregates influence the induction of PrP misfolding, neuropathology and clinical manifestations upon passage in vivo. We confirm that some rPrP aggregates can initiate further aggregation without typical pathogenesis in vivo. We also provide evidence that there is little, if any, biohazard associated with routine RT-QuIC assays.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Lisina/metabolismo
Proteínas Priônicas/metabolismo
Scrapie/metabolismo
[Mh] Termos MeSH secundário: Amiloide/química
Animais
Encéfalo/patologia
Endopeptidase K/metabolismo
Camundongos Transgênicos
Proteínas PrPSc/metabolismo
Agregados Proteicos/fisiologia
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (PrPSc Proteins); 0 (Prion Proteins); 0 (Protein Aggregates); 0 (Recombinant Proteins); EC 3.4.21.64 (Endopeptidase K); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006623


  4 / 3152 MEDLINE  
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[PMID]:28878088
[Au] Autor:Papasavva-Stylianou P; Simmons MM; Ortiz-Pelaez A; Windl O; Spiropoulos J; Georgiadou S
[Ad] Endereço:Veterinary Services, Nicosia, Cyprus.
[Ti] Título:Effect of Polymorphisms at Codon 146 of the Goat PRNP Gene on Susceptibility to Challenge with Classical Scrapie by Different Routes.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This report presents the results of experimental challenges of goats with scrapie by both the intracerebral (i.c.) and oral routes, exploring the effects of polymorphisms at codon 146 of the goat gene on resistance to disease. The results of these studies illustrate that while goats of all genotypes can be infected by i.c. challenge, the survival distribution of the animals homozygous for asparagine at codon 146 was significantly shorter than those of animals of all other genotypes (chi-square value, 10.8; = 0.001). In contrast, only those animals homozygous for asparagine at codon 146 (NN animals) succumbed to oral challenge. The results also indicate that any cases of infection in non-NN animals can be detected by the current confirmatory test (immunohistochemistry), although successful detection with the rapid enzyme-linked immunosorbent assay (ELISA) was more variable and dependent on the polymorphism. Together with data from previous studies of goats exposed to infection in the field, these data support the previously reported observations that polymorphisms at this codon have a profound effect on susceptibility to disease. It is concluded that only animals homozygous for asparagine at codon 146 succumb to scrapie under natural conditions. In goats, like in sheep, there are PRNP polymorphisms that are associated with susceptibility or resistance to scrapie. However, in contrast to the polymorphisms in sheep, they are more numerous in goats and may be restricted to certain breeds or geographical regions. Therefore, eradication programs must be specifically designed depending on the identification of suitable polymorphisms. An initial analysis of surveillance data suggested that such a polymorphism in Cypriot goats may lie in codon 146. In this study, we demonstrate experimentally that NN animals are highly susceptible after i.c. inoculation. The presence of a D or S residue prolonged incubation periods significantly, and prions were detected in peripheral tissues only in NN animals. In oral challenges, prions were detected only in NN animals, and the presence of a D or S residue at this position conferred resistance to the disease. This study provides an experimental transmission model for assessing the genetic susceptibility of goats to scrapie.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Códon
Predisposição Genética para Doença
Cabras/genética
Polimorfismo Genético
Proteínas Priônicas/genética
Scrapie/genética
[Mh] Termos MeSH secundário: Animais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (Prion Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE


  5 / 3152 MEDLINE  
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[PMID]:28758631
[Au] Autor:Carroll JA; Race B; Phillips K; Striebel JF; Chesebro B
[Ad] Endereço:Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA.
[Ti] Título:Statins are ineffective at reducing neuroinflammation or prolonging survival in scrapie-infected mice.
[So] Source:J Gen Virol;98(8):2190-2199, 2017 Aug.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Neuroinflammation is a prominent component of several neurodegenerative diseases, including multiple sclerosis, Alzheimer's disease, Parkinson's disease, tauopathies, amyotrophic lateral sclerosis and prion diseases. In such conditions, the ability to decrease neuroinflammation by drug therapy may influence disease progression. Statins have been used to treat hyperlipidemia as well as reduce neuroinflammation and oxidative stress in various tissues. In previous studies, treatment of scrapie-infected mice with the type 1 statins, simvastatin or pravastatin, showed a small beneficial effect on survival time. In the current study, to increase the effectiveness of statin therapy, we treated infected mice with atorvastatin, a type 2 statin that has improved pharmacokinetics over many type 1 statins. Treatments with either simvastatin or pravastatin were tested for comparison. We evaluated scrapie-infected mice for protease-resistant PrP (PrPres) accumulation, gliosis, neuroinflammation and time until advanced clinical disease requiring euthanasia. All three statin treatments reduced total serum cholesterol ≥40 % in mice. However, gliosis and PrPres deposition were similar in statin-treated and untreated infected mice. Time to euthanasia due to advanced clinical signs was not changed in statin-treated mice relative to untreated mice, a finding at odds with previous reports. Expression of 84 inflammatory genes involved in neuroinflammation was also quantitated. Seven genes were reduced by pravastatin, and one gene was reduced by atorvastatin. In contrast, simvastatin therapy did not reduce any of the tested genes, but did slightly increase the expression of Ccl2 and Cxcl13. Our studies indicate that none of the three statins tested were effective in reducing scrapie-induced neuroinflammation or neuropathogenesis.
[Mh] Termos MeSH primário: Doenças Neurodegenerativas/tratamento farmacológico
Doenças Neurodegenerativas/imunologia
Pravastatina/administração & dosagem
Sinvastatina/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Doenças Neurodegenerativas/mortalidade
Scrapie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
AGG2FN16EV (Simvastatin); KXO2KT9N0G (Pravastatin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000876


  6 / 3152 MEDLINE  
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[PMID]:28721847
[Au] Autor:Lacroux C; Cassard H; Simmons H; Yves Douet J; Corbière F; Lugan S; Costes P; Aron N; Huor A; Tillier C; Schelcher F; Andreoletti O
[Ad] Endereço:1​UMR INRA-ENVT 1225, 23 Chemin des Capelles, 31076 Toulouse, France.
[Ti] Título:Classical scrapie transmission in ARR/ARR genotype sheep.
[So] Source:J Gen Virol;98(8):2200-2204, 2017 Aug.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The ARR allele is considered to provide a very strong resistance against classical scrapie infection in sheep. In this study, we report the occurrence of clinical transmissible spongiform encephalopathy in ARR/ARR sheep, following their inoculation by the intracerebral route with a classical scrapie isolate. On first passage, the disease displayed an incomplete attack rate transmission, with incubation periods exceeding 6 years. On second passage, the obtained prion did not display better abilities to propagate than the original isolate. These transmission results contrasted with the 100 % attack rate and the short incubation periods observed in ARQ/ARQ sheep challenged with the same isolate. These data confirm that ARR/ARR sheep cannot be considered to be fully resistant to classical scrapie. However, they also support the contention that classical scrapie has a very limited capacity to transmit and adapt to ARR/ARR sheep.
[Mh] Termos MeSH primário: Príons/genética
Scrapie/genética
Doenças dos Ovinos/genética
Ovinos/genética
[Mh] Termos MeSH secundário: Animais
Genótipo
Camundongos
Príons/metabolismo
Scrapie/metabolismo
Scrapie/transmissão
Ovinos/metabolismo
Doenças dos Ovinos/metabolismo
Doenças dos Ovinos/transmissão
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prions)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000861


  7 / 3152 MEDLINE  
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[PMID]:28691895
[Au] Autor:Mazza M; Guglielmetti C; Ingravalle F; Brusadore S; Langeveld JPM; Ekateriniadou LV; Andréoletti O; Casalone C; Acutis PL
[Ad] Endereço:1​Italian Reference Centre for TSEs, Istituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle d'Aosta, Turin, Italy.
[Ti] Título:Low fraction of the 222K PrP variant in the protease-resistant moiety of PrPres in heterozygous scrapie positive goats.
[So] Source:J Gen Virol;98(7):1963-1967, 2017 Jul.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The presence of lysine (K) at codon 222 has been associated with resistance to classical scrapie in goats, but few scrapie cases have been identified in 222Q/K animals. To investigate the contribution of the 222K variant to PrPres formation in natural and experimental Q/K scrapie cases, we applied an immunoblotting method based on the use of two different monoclonal antibodies, F99/97.6.1 and SAF84, chosen for their different affinities to 222K and 222Q PrP variants. Our finding that PrPres seems to be formed nearly totally by the 222Q variant provides evidence that the 222K PrP variant confers resistance to conversion to PrPres formation and reinforces the view that this mutation has a protective role against classical scrapie in goats.
[Mh] Termos MeSH primário: Doenças das Cabras/metabolismo
Lisina/metabolismo
Proteínas PrPSc/metabolismo
Scrapie/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Códon/genética
Códon/metabolismo
Genótipo
Cabras
Lisina/genética
Peptídeo Hidrolases/metabolismo
Proteínas PrPSc/química
Proteínas PrPSc/genética
Scrapie/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (PrPSc Proteins); EC 3.4.- (Peptide Hydrolases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000843


  8 / 3152 MEDLINE  
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[PMID]:28636656
[Au] Autor:Miyazawa K; Masujin K; Okada H; Ushiki-Kaku Y; Matsuura Y; Yokoyama T
[Ad] Endereço:Prion Diseases Unit, Division of Transboundary Animal Disease, National Institute of Animal Health, National Agriculture and Food Research Organization (NARO), Tsukuba, Ibaraki, Japan.
[Ti] Título:Selective propagation of mouse-passaged scrapie prions with long incubation period from a mixed prion population using GT1-7 cells.
[So] Source:PLoS One;12(6):e0179317, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In our previous study, we demonstrated the propagation of mouse-passaged scrapie isolates with long incubation periods (L-type) derived from natural Japanese sheep scrapie cases in murine hypothalamic GT1-7 cells, along with disease-associated prion protein (PrPSc) accumulation. We here analyzed the susceptibility of GT1-7 cells to scrapie prions by exposure to infected mouse brains at different passages, following interspecies transmission. Wild-type mice challenged with a natural sheep scrapie case (Kanagawa) exhibited heterogeneity of transmitted scrapie prions in early passages, and this mixed population converged upon one with a short incubation period (S-type) following subsequent passages. However, when GT1-7 cells were challenged with these heterologous samples, L-type prions became dominant. This study demonstrated that the susceptibility of GT1-7 cells to L-type prions was at least 105 times higher than that to S-type prions and that L-type prion-specific biological characteristics remained unchanged after serial passages in GT1-7 cells. This suggests that a GT1-7 cell culture model would be more useful for the economical and stable amplification of L-type prions at the laboratory level. Furthermore, this cell culture model might be used to selectively propagate L-type scrapie prions from a mixed prion population.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Hipotálamo/metabolismo
Proteínas PrPSc/metabolismo
Príons/isolamento & purificação
Scrapie/transmissão
[Mh] Termos MeSH secundário: Animais
Encéfalo/citologia
Células Cultivadas
Hipotálamo/citologia
Camundongos
Camundongos Endogâmicos ICR
Príons/metabolismo
Príons/patogenicidade
Scrapie/metabolismo
Scrapie/patologia
Inoculações Seriadas
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PrPSc Proteins); 0 (Prions)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179317


  9 / 3152 MEDLINE  
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[PMID]:28613153
[Au] Autor:Hanusova Z; Mosko T; Matej R; Holada K
[Ad] Endereço:1​Institute of Immunology and Microbiology, First Faculty of Medicine, Charles University, Studnickova 7, Prague 2, 128 00, Czech Republic.
[Ti] Título:Precision in the design of an experimental study deflects the significance of proteinase-activated receptor 2 expression in scrapie-inoculated mice.
[So] Source:J Gen Virol;98(6):1563-1569, 2017 Jun.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Proteinase-activated receptor 2 (PAR2) is suspected to modulate the pathogenesis of various neurodegenerative conditions. We previously described delayed onset of clinical symptoms and prolonged survival of PAR2-deficient mice after intracerebral inoculation with prions. Here we report the results from a refined blinded study that aimed to investigate the effects of PAR2 deletion on scrapie pathogenesis after peripheral infection. This study failed to confirm that PAR2 deficiency impacts on the length of the incubation period, with PAR2-/- and PAR2+/+ littermates developing scrapie at the same time. To clarify the discrepancy between the two observations, we repeated the intracerebral inoculation study while utilizing our refined protocol, which aimed to limit possible sources of experimental bias. The study again failed to confirm the significant effect of PAR2 expression on the course of prion infection. Our report emphasizes and discusses the importance of unbiased experimental design and the selection of proper genetic controls when using genetically altered animal models for prion pathogenesis studies.
[Mh] Termos MeSH primário: Receptor PAR-2/metabolismo
Scrapie/fisiopatologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Feminino
Camundongos
Camundongos Knockout
Receptor PAR-2/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptor, PAR-2)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000803


  10 / 3152 MEDLINE  
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[PMID]:28605958
[Au] Autor:Kim YC; Jeong BH
[Ad] Endereço:Korea Zoonosis Research Institute, Chonbuk National University , 820-120, Hana-ro, Iksan, Jeonbuk 570-390 , Republic of Korea.
[Ti] Título:The first report of prion-related protein gene (PRNT) polymorphisms in goat.
[So] Source:Acta Vet Hung;65(2):291-300, 2017 06.
[Is] ISSN:0236-6290
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo: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.
[Mh] Termos MeSH primário: Doenças das Cabras/genética
Polimorfismo de Nucleotídeo Único
Príons/genética
Scrapie/genética
[Mh] Termos MeSH secundário: Animais
DNA/genética
Cabras
Haplótipos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Prions); 9007-49-2 (DNA)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170614
[St] Status:MEDLINE
[do] DOI:10.1556/004.2017.028



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