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https://www.readbyqxmd.com/read/29155968/novel-spiroplasma-spp-cultured-from-brains-and-lymph-nodes-from-ruminants-affected-with-transmissible-spongiform-encephalopathy
#1
Frank O Bastian, James Lynch, Sue Hagius, Xiaochu Wu, Greg McCormick, Donald G Luther, Philip H Elzer
Spiroplasma spp., tiny filterable wall-less bacteria, are consistently associated with the transmissible spongiform encephalopathies (TSE). Spiral forms have been transiently isolated from TSE-affected brain tissues in SP4 growth media designed for isolation of Spiroplasma spp., but the isolate could not be propagated in SP4 media. A bacterium must grow in vitro in cell-free cultures to allow full characterization of a suspect pathogen. Here, a novel Spiroplasma sp. was isolated from scrapie- and chronic wasting disease (CWD)-affected brains and lymph nodes...
November 15, 2017: Journal of Neuropathology and Experimental Neurology
https://www.readbyqxmd.com/read/29107182/identification-of-the-internal-ribosome-entry-sites-ires-of-prion-protein-gene
#2
Xiao-Nuan Luo, Qin-Qin Song, Jie Yu, Juan Song, Xin-Ling Wang, Dong Xia, Peng Sun, Jun Han
Many studies demonstrated that there are several type bands of prion protein in cells. However, the formation of different prion protein bands is elusive. After several low molecular weight bands of prion protein appeared in SMB-S15 cells infected with scrapie agent Chandler, we think that IRES-dependent translation mechanism induced by prion is involved in the formation of prion protein bands. Then we designed a series of pPrP-GFP fusing plasmids and bicistronic plasmids to identify the IRES sites of prion protein gene and found 3 IRES sites inside of PrP mRNA...
October 26, 2017: International Journal of Biochemistry & Cell Biology
https://www.readbyqxmd.com/read/29069734/mgr1-antigen-37-kda-laminin-receptor-precursor-promotes-cellular-prion-protein-induced-multi-drug-resistance-of-gastric-cancer
#3
Guanhong Luo, Weijie Wang, Qiong Wu, Yuanyuan Lu, Tao Su, Nan Gu, Kai Li, Jingbo Wang, Rui Du, Xiaodi Zhao, Xiaohua Li, Rui Fan, Hongbo Zhang, Yongzhan Nie, Xinmin Zhou, Yongquan Shi, Jie Liang, Xin Wang, Daiming Fan
Cellular prion protein (PrP(C)), the infective agent of transmissible spongiform encephalopathies, is thought to be related to several cellular physiological and physiopathological processes. We have previously reported that PrP(C) participates in multi-drug-resistance of gastric cancer. As the salient ligand molecule of PrP for participating in internalization and propagation of the scrapie form of prion protein (PrP(Sc)), 37 kDa laminin receptor precursor protein (37LRP) shared the same gene coding sequence of MGr1-Ag, another protein previously found to be involved in multi-drug-resistance of gastric cancer in our lab...
September 22, 2017: Oncotarget
https://www.readbyqxmd.com/read/29058651/estimating-chronic-wasting-disease-susceptibility-in-cervids-using-real-time-quaking-induced-conversion
#4
Nicholas J Haley, Rachel Rielinger, Kristen A Davenport, Katherine O'Rourke, Gordon Mitchell, Jürgen A Richt
In mammals, susceptibility to prion infection is primarily modulated by the host's cellular prion protein (PrP(C)) sequence. In the sheep scrapie model, a graded scale of susceptibility has been established both in vivo and in vitro based on PrP(C) amino acids 136, 154 and 171, leading to global breeding programmes to reduce the prevalence of scrapie in sheep. Chronic wasting disease (CWD) resistance in cervids is often characterized as decreased prevalence and/or protracted disease progression in individuals with specific alleles; at present, no PrP(C) allele conferring absolute resistance in cervids has been identified...
November 2017: Journal of General Virology
https://www.readbyqxmd.com/read/29046443/prion-protein-devoid-of-the-octapeptide-repeat-region-delays-bse-pathogenesis-in-mice
#5
Hideyuki Hara, Hironori Miyata, Nandita Rani Das, Junji Chida, Tatenobu Yoshimochi, Keiji Uchiyama, Hitomi Watanabe, Gen Kondoh, Takashi Yokoyama, Suehiro Sakaguchi
Conformational conversion of the cellular isoform of prion protein PrP(C), into the abnormally folded, amyloidogenic isoform, PrP(Sc), is a key pathogenic event in prion diseases including Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy (BSE) in animals. We previously reported that the octapeptide repeat (OR) region could be dispensable for converting PrP(C) into PrP(Sc) after infection with RML prions. We demonstrated that mice transgenically expressing mouse PrP with deletion of the OR region on the PrP-knockout background, designated Tg(PrPΔOR)/Prnp(0/0) mice, did not reduce susceptibility to RML scrapie prions, with abundant accumulation of PrP(Sc)ΔOR in their brains...
October 18, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28968141/aberrant-alterations-of-the-expressions-and-s-nitrosylation-of-calmodulin-and-the-downstream-factors-in-the-brains-of-the-rodents-during-scrapie-infection
#6
Ren-Qing Zhang, Cao Chen, Li-Jie Xiao, Jing Sun, Yue Ma, Xiao-Dong Yang, Xiao-Feng Xu, Kang Xiao, Qi Shi, Zhi-Bao Chen, Xiao-Ping Dong
The aberrant alterations of calmodulin (CaM) and its downstream substrates have been reported in some neurodegenerative diseases, but rarely described in prion disease. In this study, the potential changes of Ca(2+)/CaM and its associated agents in the brains of scrapie agent 263K-infected hamsters and the prion infected cell line SMB-S15 were evaluated by various methodologies. We found that the level of CaM in the brains of 263K-infected hamsters started to increase at early stage and maintained at high level till terminal stage...
September 3, 2017: Prion
https://www.readbyqxmd.com/read/28956708/remarkable-increases-of-%C3%AE-1-antichymotrypsin-in-brain-tissues-of-rodents-during-prion-infection
#7
Cao Chen, Xiao-Feng Xu, Ren-Qing Zhang, Yue Ma, Yan Lv, Jian-Le Li, Qiang Shi, Kang Xiao, Jing Sun, Xiao-Dong Yang, Qi Shi, Xiao-Ping Dong
α1-Antichymotrypsin (α1-ACT) belongs to a kind of acute-phase inflammatory protein. Recently, such protein has been proved exist in the amyloid deposits which is the hallmark of Alzheimer's disease, but limitedly reported in prion disease. To estimate the change of α1-ACT during prion infection, the levels of α1-ACT in the brain tissues of scrapie agents 263K-, 139A- and ME7-infected rodents were analyzed, respectively. Results shown that α1-ACT levels were significantly increased in the brain tissues of the three kinds of scrapie-infected rodents, displaying a time-dependent manner during prion infection...
September 3, 2017: Prion
https://www.readbyqxmd.com/read/28942337/a-novel-approach-for-scrapie-associated-prion-prp-sc-detection-in-blood-using-the-competitive-affinity-of-an-aggregate-specific-antibody-and-streptavidin-to-prp-sc
#8
Andrei Soutyrine, Hongsheng Huang, Olga Andrievskaia, Ines Walther, Gordon Mitchell
Scrapie is a fatal neurodegenerative disorder affecting sheep and goats, originating from exposure to disease-associated prions (PrP(Sc)). An ante-mortem screening test that can detect native PrP(Sc) in body fluids remains unavailable due to insufficient sensitivity of current detection methods that involve proteinase or denaturation treatments. We adopted an approach to detect PrP(Sc) in whole blood using a simple proteinase- and denaturation-independent immunoassay, based on the competitive affinity of an aggregate-specific monoclonal antibody and streptavidin to PrP(Sc)...
September 9, 2017: Research in Veterinary Science
https://www.readbyqxmd.com/read/28927447/protecting-effect-of-prp-codons-m142-and-k222-in-goats-orally-challenged-with-bovine-spongiform-encephalopathy-prions
#9
C Fast, W Goldmann, P Berthon, K Tauscher, O Andréoletti, I Lantier, C Rossignol, A Bossers, J G Jacobs, N Hunter, M H Groschup, F Lantier, J P M Langeveld
Breeding towards genetic resistance to prion disease is effective in eliminating scrapie. In sheep, classical forms of scrapie have been eradicated almost completely in several countries by breeding programs using a prion protein (PrP) gene (PRNP) amino acid polymorphism. For goats, field and experimental studies have provided evidence for several amino acid polymorphisms that are associated with resistance to scrapie, but only limited data are available concerning the susceptibility of caprine PRNP genotypes to BSE...
September 19, 2017: Veterinary Research
https://www.readbyqxmd.com/read/28920852/experimental-transmission-to-a-calf-of-an-isolate-of-spanish-classical-scrapie
#10
Rosa Bolea, Carlos Hedman, Óscar López-Pérez, Belén Marín, Enríc Vidal, Martí Pumarola, Fabien Corbière, Antonio Romero, Bernardino Moreno, Inmaculada Martín-Burriel, Olivier Andréoletti, Juan José Badiola
Multiple theories exist regarding the origin of bovine spongiform encephalopathy (BSE). An early and prominent theory proposed that BSE was the result of the adaptation of sheep scrapie to cattle. The reports to date indicate that the distribution of the pathological prion protein (PrPSc) in experimental bovine scrapie is largely restricted to the central nervous system (CNS). Here, we describe pathological findings in a calf intracerebrally inoculated with a Spanish classical scrapie isolate. While clinical disease was observed 30 months after inoculation and PrPSc was detected in the CNS, the corresponding phenotype differed from that of BSE...
September 18, 2017: Journal of General Virology
https://www.readbyqxmd.com/read/28910420/role-of-the-central-lysine-cluster-and-scrapie-templating-in-the-transmissibility-of-synthetic-prion-protein-aggregates
#11
Bradley R Groveman, Gregory J Raymond, Katrina J Campbell, Brent Race, Lynne D Raymond, Andrew G Hughson, Christina D Orrú, Allison Kraus, Katie Phillips, Byron Caughey
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...
September 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28906181/a-decade-of-using-small-to-medium-throughput-allele-discrimination-assay-to-determine-prion-protein-gene-prnp-genotypes-in-sheep-in-slovenia
#12
Jelka Zabavnik, Marko Cotman, Polona Juntes, Ivan Ambrozic
Sheep with valine (V) at codon 136 and glutamine (Q) at codon 171 of the prion protein gene ( Prnp) are highly susceptible to classical scrapie, whereas phenylalanine (F) at codon 141 and histidine (H) at codon 154 play a major role in the susceptibility to atypical scrapie. A TaqMan real-time PCR assay was developed to determine Prnp alleles at codons 136, 141, 154, and 171 and used in classical scrapie eradication and breeding programs adopted in Slovenia. The frequency of the most resistant genotypes ARR/ARR and ARR/ARQ increased significantly in tested animals ( n = 35,138) from 6...
September 1, 2017: Journal of Veterinary Diagnostic Investigation
https://www.readbyqxmd.com/read/28878088/effect-of-polymorphisms-at-codon-146-of-the-goat-prnp-gene-on-susceptibility-to-challenge-with-classical-scrapie-by-different-routes
#13
Penelope Papasavva-Stylianou, Marion Mathieson Simmons, Angel Ortiz-Pelaez, Otto Windl, John Spiropoulos, Soteria Georgiadou
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 PRNP 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...
November 15, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28861790/methods-of-protein-misfolding-cyclic-amplification
#14
Natallia Makarava, Regina Savtchenko, Ilia V Baskakov
Protein misfolding cyclic amplification (PMCA) amplifies infectious prions in vitro. Over the past decade, PMCA has become an essential tool in prion research. The current chapter describes in detail the PMCA format with beads (PMCAb) and several methods that rely on PMCAb for assessing strain-specific prion amplification rates, for selective amplification of subtypes of PrP(Sc) from a mixture, and a PMCAb approach that can replace animal titration of scrapie material. Development of PMCAb-based methodology is important for addressing a number of research topics including prion strain evolution, selection and adaptation, strain-typing, prion detection, and biochemical requirements for prion replication...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28855681/%C3%AE-synuclein-amyloids-hijack-prion-protein-to-gain-cell-entry-facilitate-cell-to-cell-spreading-and-block-prion-replication
#15
Suzana Aulić, Lara Masperone, Joanna Narkiewicz, Elisa Isopi, Edoardo Bistaffa, Elena Ambrosetti, Beatrice Pastore, Elena De Cecco, Denis Scaini, Paola Zago, Fabio Moda, Fabrizio Tagliavini, Giuseppe Legname
The precise molecular mechanism of how misfolded α-synuclein (α-Syn) accumulates and spreads in synucleinopathies is still unknown. Here, we show the role of the cellular prion protein (PrP(C)) in mediating the uptake and the spread of recombinant α-Syn amyloids. The in vitro data revealed that the presence of PrP(C) fosters the higher uptake of α-Syn amyloid fibrils, which was also confirmed in vivo in wild type (Prnp (+/+)) compared to PrP knock-out (Prnp (-/-)) mice. Additionally, the presence of α-Syn amyloids blocked the replication of scrapie prions (PrP(Sc)) in vitro and ex vivo, indicating a link between the two proteins...
August 30, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28851903/prion-protein-facilitates-retinal-iron-uptake-and-is-cleaved-at-the-%C3%AE-site-implications-for-retinal-iron-homeostasis-in-prion-disorders
#16
Abhishek Asthana, Shounak Baksi, Ajay Ashok, Shilpita Karmakar, Najiba Mammadova, Robyn Kokemuller, Mary Heather Greenlee, Qingzhong Kong, Neena Singh
Prion disease-associated retinal degeneration is attributed to PrP-scrapie (PrP(Sc)), a misfolded isoform of prion protein (PrP(C)) that accumulates in the neuroretina. However, a lack of temporal and spatial correlation between PrP(Sc) and cytotoxicity suggests the contribution of host factors. We report retinal iron dyshomeostasis as one such factor. PrP(C) is expressed on the basolateral membrane of retinal-pigment-epithelial (RPE) cells, where it mediates uptake of iron by the neuroretina. Accordingly, the neuroretina of PrP-knock-out mice is iron-deficient...
August 29, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28838667/the-structure-of-the-infectious-prion-protein-and-its-propagation
#17
Jesús R Requena, Holger Wille
The prion diseases, which include Creutzfeldt-Jakob disease in humans, chronic wasting disease in cervids (i.e., deer, elk, moose, and reindeer), bovine spongiform encephalopathy in cattle, as well as sheep and goat scrapie, are caused by the conversion of the cellular prion protein (PrP(C)) into a disease-causing conformer (PrP(Sc)). PrP(C) is a regular, GPI-anchored protein that is expressed on the cell surface of neurons and many other cell types. The structure of PrP(C) is well studied, based on analyses of recombinant PrP, which is thought to mimic the structure of native PrP(C)...
2017: Progress in Molecular Biology and Translational Science
https://www.readbyqxmd.com/read/28838664/scrapie-cwd-and-transmissible-mink-encephalopathy
#18
Candace K Mathiason
Transmissible spongiform encephalopathies (TSEs), or prions, are neurodegenerative diseases that affect a variety of animal species, including humans. Cruetzfeldt-Jakob disease (CJD) in humans, sheep and goat scrapie, chronic wasting disease (CWD) of cervids, and transmissible mink encephalopathy (TME) of mink are classified as TSEs. According to the "protein-only" hypothesis (Prusiner, 1982),(1) prions are devoid of nucleic acids and consist of assemblies of misfolded host-encoded normal protein, the prion protein (PrP(C))...
2017: Progress in Molecular Biology and Translational Science
https://www.readbyqxmd.com/read/28838658/prion-protein-and-genetic-susceptibility-to-diseases-caused-by-its-misfolding
#19
George A Carlson
Early genetic studies on scrapie, an infectious neurodegenerative disease of sheep that was adapted to mice, provided evidence in support of the hypothesis that the agent was a slow virus with a nucleic acid genome independent of the host. Particularly compelling support for an independent genome came from the existence of strains of scrapie agent, some of which were true breeding, while others appeared to mutate under selective pressure. Kuru, a neurodegenerative disease in the remote highlands of Papua New Guinea, had pathological changes similar to those in scrapie and also proved to be transmissible...
2017: Progress in Molecular Biology and Translational Science
https://www.readbyqxmd.com/read/28835493/prp-p102l-and-nearby-lysine-mutations-promote-spontaneous-in-vitro-formation-of-transmissible-prions
#20
Allison Kraus, Gregory J Raymond, Brent Race, Katrina J Campbell, Andrew G Hughson, Kelsie J Anson, Lynne D Raymond, Byron Caughey
Accumulation of fibrillar protein aggregates is a hallmark of many diseases. While numerous proteins form fibrils by prion-like seeded polymerization in vitro, only some are transmissible and pathogenic in vivo To probe the structural features that confer transmissibility to prion protein (PrP) fibrils, we have analyzed synthetic PrP amyloids with or without the human prion disease-associated P102L mutation. The formation of infectious prions from PrP molecules in vitro has required cofactors and/or unphysiological denaturing conditions...
November 1, 2017: Journal of Virology
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