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https://www.readbyqxmd.com/read/28820384/chronic-wasting-disease-prion-strain-emergence-and-host-range-expansion
#1
Allen Herbst, Camilo Duque Velásquez, Elizabeth Triscott, Judd M Aiken, Debbie McKenzie
Human and mouse prion proteins share a structural motif that regulates resistance to common chronic wasting disease (CWD) prion strains. Successful transmission of an emergent strain of CWD prion, H95(+), into mice resulted in infection. Thus, emergent CWD prion strains may have higher zoonotic potential than common strains.
September 2017: Emerging Infectious Diseases
https://www.readbyqxmd.com/read/28820136/protective-effect-of-val129-prp-against-bovine-spongiform-encephalopathy-but-not-variant-creutzfeldt-jakob-disease
#2
Natalia Fernández-Borges, Juan Carlos Espinosa, Alba Marín-Moreno, Patricia Aguilar-Calvo, Emmanuel A Asante, Tetsuyuki Kitamoto, Shirou Mohri, Olivier Andréoletti, Juan María Torres
Bovine spongiform encephalopathy (BSE) is the only known zoonotic prion that causes variant Creutzfeldt-Jakob disease (vCJD) in humans. The major risk determinant for this disease is the polymorphic codon 129 of the human prion protein (Hu-PrP), where either methionine (Met129) or valine (Val129) can be encoded. To date, all clinical and neuropathologically confirmed vCJD cases have been Met129 homozygous, with the exception of 1 recently reported Met/Val heterozygous case. Here, we found that transgenic mice homozygous for Val129 Hu-PrP show severely restricted propagation of the BSE prion strain, but this constraint can be partially overcome by adaptation of the BSE agent to the Met129 Hu-PrP...
September 2017: Emerging Infectious Diseases
https://www.readbyqxmd.com/read/28817974/applications-of-the-real-time-quaking-induced-conversion-assay-in-diagnosis-prion-strain-typing-drug-pre-screening-and-other-amyloidopathies
#3
Niccolò Candelise, Matthias Schmitz, Susana Margarida da Silva Correia, Aman Arora, Anna Villar-Piqué, Saima Zafar, Franc Llorens, Maria Cramm, Inga Zerr
The development of in vitro protein misfolding amplification assays for the detection and analysis of abnormally folded proteins, such as proteinase K resistant prion protein (PrP(res)) was a major innovation in the prion field. In prion diseases, these types of assays imitate the pathological conversion of the cellular PrP (PrP(C)) into a proteinase resistant associated conformer or amyloid, called PrP(res). Areas covered: The most prominent protein misfolding amplification assays are the protein misfolding cyclic amplification (PMCA), which is based on sonication and the real-time quaking-induced conversion (RT-QuIC) technique based on shaking...
August 18, 2017: Expert Review of Molecular Diagnostics
https://www.readbyqxmd.com/read/28817252/experimental-and-theoretical-insights-into-the-inhibition-mechanism-of-prion-fibrillation-by-resveratrol-and-its-derivatives
#4
Lanlan Li, Yongchang Zhu, Shuangyan Zhou, Xiaoli An, Yan Zhang, Qifeng Bai, Yong-Xing He, Huanxiang Liu, Xiao-Jun Yao
Resveratrol and its derivatives have been shown to display beneficial effects to neurodegenerative diseases. However, the molecular mechanism of resveratrol and its derivatives on prion conformational conversion is poorly understood. In this work, the interaction mechanism between prion and resveratrol as well as its derivatives were investigated using steady-state fluorescence quenching, Thioflavin T binding assay, western blotting and molecular dynamics simulation. Protein fluorescence quenching method and Thioflavin T assay revealed that resveratrol and its derivatives could interact with prion and interrupt prion fibrils formation...
August 17, 2017: ACS Chemical Neuroscience
https://www.readbyqxmd.com/read/28814753/the-psi-yeast-prion-does-not-wildly-affect-proteome-composition-whereas-selective-pressure-exerted-on-psi-cells-can-promote-aneuploidy
#5
Patrick H W Chan, Lisa Lee, Erin Kim, Tony Hui, Nikolay Stoynov, Roy Nassar, Michelle Moksa, Dale M Cameron, Martin Hirst, Joerg Gsponer, Thibault Mayor
The yeast Sup35 protein is a subunit of the translation termination factor, and its conversion to the [PSI (+)] prion state leads to more translational read-through. Although extensive studies have been done on [PSI (+)], changes at the proteomic level have not been performed exhaustively. We therefore used a SILAC-based quantitative mass spectrometry approach and identified 4187 proteins from both [psi (-)] and [PSI (+)] strains. Surprisingly, there was very little difference between the two proteomes under standard growth conditions...
August 16, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28814578/genetic-human-prion-disease-modelled-in-prp-transgenic-drosophila
#6
Alana M Thackray, Alzbeta Cardova, Hanna Wolf, Lydia Pradl, Ina Vorberg, Walker S Jackson, Raymond Bujdoso
Inherited human prion diseases, such as FFI and familial CJD (fCJD), are associated with autosomal dominant mutations in the human prion protein gene PRNP and accumulation of PrPSc, an abnormal isomer of the normal host protein PrPC, in the brain of affected individuals. PrPSc is the principal component of the transmissible neurotoxic prion agent. It is important to identify molecular pathways and cellular processes that regulate prion formation and prion-induced neurotoxicity. This will allow identification of possible therapeutic interventions for individuals with, or at risk from, genetic human prion disease...
August 16, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28811866/preliminary-data-on-the-interaction-between-some-biometals-and-oxidative-stress-status-in-mild-cognitive-impairment-and-alzheimer-s-disease-patients
#7
Ioana-Miruna Balmuș, Stefan-Adrian Strungaru, Alin Ciobica, Mircea-Nicusor Nicoara, Romeo Dobrin, Gabriel Plavan, Cristinel Ștefănescu
Increased interest regarding the biometal mechanisms of action and the pathways in which they have regulatory roles was lately observed. Particularly, it was shown that biometal homeostasis dysregulation may lead to neurodegeneration including Alzheimer's disease, Parkinson disease, or prion protein disease, since important molecular signaling mechanisms in brain functions implicate both oxidative stress and redox active biometals. Oxidative stress could be a result of a breakdown in metal-ion homeostasis which leads to abnormal metal protein chelation...
2017: Oxidative Medicine and Cellular Longevity
https://www.readbyqxmd.com/read/28811267/app-a%C3%AE-structural-diversity-and-alzheimer-s-disease-pathogenesis
#8
REVIEW
Alex E Roher, Tyler A Kokjohn, Steven G Clarke, Michael R Sierks, Chera L Maarouf, Geidy E Serrano, Marwan S Sabbagh, Thomas G Beach
The amyloid cascade hypothesis of Alzheimer's disease (AD) proposes amyloid- β (Aβ) is a chief pathological element of dementia. AD therapies have targeted monomeric and oligomeric Aβ 1-40 and 1-42 peptides. However, alternative APP proteolytic processing produces a complex roster of Aβ species. In addition, Aβ peptides are subject to extensive posttranslational modification (PTM). We propose that amplified production of some APP/Aβ species, perhaps exacerbated by differential gene expression and reduced peptide degradation, creates a diverse spectrum of modified species which disrupt brain homeostasis and accelerate AD neurodegeneration...
August 12, 2017: Neurochemistry International
https://www.readbyqxmd.com/read/28809826/high-throughput-screening-for-protein-based-inheritance-in-s-cerevisiae
#9
James S Byers, Daniel F Jarosz
The encoding of biological information that is accessible to future generations is generally achieved via changes to the DNA sequence. Long-lived inheritance encoded in protein conformation (rather than sequence) has long been viewed as paradigm-shifting but rare. The best characterized examples of such epigenetic elements are prions, which possess a self-assembling behavior that can drive the heritable manifestation of new phenotypes. Many archetypal prions display a striking N/Q-rich sequence bias and assemble into an amyloid fold...
August 8, 2017: Journal of Visualized Experiments: JoVE
https://www.readbyqxmd.com/read/28805003/protein-astrogliopathies-in-human-neurodegenerative-diseases-and-aging
#10
Gabor G Kovacs, Virginia M Lee, John Q Trojanowski
Neurodegenerative diseases are characterized by progressive dysfunction and loss of neurons associated with depositions of pathologically altered proteins showing hierarchical involvement of brain regions. The role of astrocytes in the pathogenesis of neurodegenerative diseases is explored as contributors to neuronal degeneration or neuroprotection pathways, and also as potential mediators of the transcellular spreading of disease-associated proteins. Protein astrogliopathy (PAG), including deposition of amyloid-β, prion protein, tau, α-synuclein, and very rarely transactive response DNA-binding protein 43 (TDP-43) is not unprecedented or unusual in neurodegenerative diseases...
September 2017: Brain Pathology
https://www.readbyqxmd.com/read/28803412/alpha-synuclein-oligomers-a-new-hope
#11
REVIEW
Nora Bengoa-Vergniory, Rosalind F Roberts, Richard Wade-Martins, Javier Alegre-Abarrategui
Alpha-synuclein is a protein implicated in Parkinson's disease and thought to be one of the main pathological drivers in the disease, although it remains unclear how this protein elicits its neurotoxic effects. Recent findings indicate that the assembly of toxic oligomeric species of alpha-synuclein may be one of the key processes for the pathology and spread of the disease. The absence of a sensitive in situ detection method has hindered the study of these oligomeric species and the role they play in the human brain until recently...
August 12, 2017: Acta Neuropathologica
https://www.readbyqxmd.com/read/28800967/role-of-prion-protein-in-premature-senescence-of-human-fibroblasts
#12
Emmanuelle Boilan, Virginie Winant, Elise Dumortier, Benaissa ElMoualij, Pascale Quatresooz, Heinz D Osiewacz, Florence Debacq-Chainiaux, Olivier Toussaint
Prion protein (PrP) is essentially known for its capacity to induce neurodegenerative prion diseases in mammals caused by a conformational change in its normal cellular isoform (PrP(C)) into an infectious and disease-associated misfolded form, called scrapie isoform (PrP(Sc)). Although its sequence is highly conserved, less information is available on its physiological role under normal conditions. However, increasing evidence supports a role for PrP(C) in the cellular response to oxidative stress. In the present study, a new link between PrP and senescence is highlighted...
August 8, 2017: Mechanisms of Ageing and Development
https://www.readbyqxmd.com/read/28800624/destabilizing-polymorphism-in-cervid-prion-protein-hydrophobic-core-determines-prion-conformation-and-conversion-efficiency
#13
Samia Hannaoui, Sara Amidian, Yo Ching Cheng, Camilo Duque Velásquez, Lyudmyla Dorosh, Sampson Law, Glenn Telling, Maria Stepanova, Debbie McKenzie, Holger Wille, Sabine Gilch
Prion diseases are infectious neurodegenerative disorders of humans and animals caused by misfolded forms of the cellular prion protein PrPC. Prions cause disease by converting PrPC into aggregation-prone PrPSc. Chronic wasting disease (CWD) is the most contagious prion disease with substantial lateral transmission, affecting free-ranging and farmed cervids. Although the PrP primary structure is highly conserved among cervids, the disease phenotype can be modulated by species-specific polymorphisms in the prion protein gene...
August 11, 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28797122/cross-seeding-of-prions-by-aggregated-%C3%AE-synuclein-leads-to-transmissible-spongiform-encephalopathy
#14
Elizaveta Katorcha, Natallia Makarava, Young Jin Lee, Iris Lindberg, Mervyn J Monteiro, Gabor G Kovacs, Ilia V Baskakov
Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases. Recent years have witnessed a growing number of reports of overlap in neuropathological features that were once thought to be unique to only one neurodegenerative disorder. However, the origin for the overlap remains unclear. One possibility is that diseases with mixed brain pathologies might arise from cross-seeding of one amyloidogenic protein by aggregated states of unrelated proteins...
August 10, 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28795797/molecular-dynamics-simulations-study-on-the-binding-and-stabilization-mechanism-of-antiprion-compounds-to-the-hot-spot-region-of-prpc
#15
Shuangyan Zhou, Xuewei Liu, Xiaoli An, Xiao-Jun Yao, Huanxiang Liu
Structural transitions in the prion protein from the cellular form, PrPC, into the pathological isoform, PrPSc, are regarded as the main cause of the transmissible spongiform encephalopathies, also known as prion diseases. Hence, discovering and designing effective antiprion drugs that can inhibit PrPC to PrPSc conversion is regarded as a promising way to cure prion disease. Among several strategies to inhibit PrPC to PrPSc conversion, to stabilize the native PrPC via specific binding is believed to be one of the valuable approach and many antiprion compounds have been reported based on this strategy...
August 10, 2017: ACS Chemical Neuroscience
https://www.readbyqxmd.com/read/28794434/protective-role-of-cellular-prion-protein-against-tnf%C3%AE-mediated-inflammation-through-tace-%C3%AE-secretase
#16
Juliette Ezpeleta, François Boudet-Devaud, Mathéa Pietri, Anne Baudry, Vincent Baudouin, Aurélie Alleaume-Butaux, Nathalie Dagoneau, Odile Kellermann, Jean-Marie Launay, Benoit Schneider
Although cellular prion protein PrP(C) is well known for its implication in Transmissible Spongiform Encephalopathies, its functions remain elusive. Combining in vitro and in vivo approaches, we here show that PrP(C) displays the intrinsic capacity to protect neuronal cells from a pro-inflammatory TNFα noxious insult. Mechanistically, PrP(C) coupling to the NADPH oxidase-TACE α-secretase signaling pathway promotes TACE-mediated cleavage of transmembrane TNFα receptors (TNFRs) and the release of soluble TNFR, which limits the sensitivity of recipient cells to TNFα...
August 9, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28791742/a-multispecific-monoclonal-antibody-g2-recognizes-at-least-three-completely-different-epitope-sequences-with-high-affinity
#17
Md Nuruddin Mahmud, Masayuki Oda, Daiki Usui, Yasuo Inoshima, Naotaka Ishiguro, Yuji O Kamatari
A monoclonal antibody (mAb) G2 possesses an unusual characteristic of reacting with at least three proteins (ATP6V1C1, SEPT3, and C6H10orf76) other than its original antigen, chicken prion protein (ChPrP). The epitopes on ChPrP and ATP6V1C1 have been identified previously. In this study, we identified the epitope in the third protein, SEPT3. Interestingly, there was no amino acid sequence similarity among the epitopes on the three proteins. These epitopes had high binding affinities to G2 (KD = ∼10(-7) M for monovalent binding and KD = ∼10(-9) M for divalent binding), as determined using a SPR biosensor...
August 9, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28791720/infectivity-in-bone-marrow-from-sporadic-cjd-patients
#18
Alvina Huor, Jean Yves Douet, Caroline Lacroux, Séverine Lugan, Cécile Tillier, Naima Aron, Hervé Cassard, Mark Arnold, Juan Maria Torres, James W Ironside, Olivier Andréoletti
Prion infectivity was recently identified in the blood of both sporadic and variant Creutzfeldt-Jakob disease (CJD) patients. In variant CJD (vCJD) the widespread distribution of prions in peripheral tissues of both asymptomatic and symptomatic patients is likely to explain the occurrence of the observed prionaemia. However, in sporadic CJD (sCJD) prion infectivity is described to be located principally in the central nervous system. In this study, we investigated the presence of prion infectivity in bone marrow collected after death in patients affected with different sCJD agents...
August 9, 2017: Journal of Pathology
https://www.readbyqxmd.com/read/28790319/novel-animal-model-defines-genetic-contributions-for-neuron-to-neuron-transfer-of-%C3%AE-synuclein
#19
Trevor Tyson, Megan Senchuk, Jason F Cooper, Sonia George, Jeremy M Van Raamsdonk, Patrik Brundin
Cell-to-cell spreading of misfolded α-synuclein (α-syn) is suggested to contribute to the progression of neuropathology in Parkinson's disease (PD). Compelling evidence supports the hypothesis that misfolded α-syn transmits from neuron-to-neuron and seeds aggregation of the protein in the recipient cells. Furthermore, α-syn frequently appears to propagate in the brains of PD patients following a stereotypic pattern consistent with progressive spreading along anatomical pathways. We have generated a C. elegans model that mirrors this progression and allows us to monitor α-syn neuron-to-neuron transmission in a live animal over its lifespan...
August 8, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28790177/phosphorylation-of-the-fus-low-complexity-domain-disrupts-phase-separation-aggregation-and-toxicity
#20
Zachary Monahan, Veronica H Ryan, Abigail M Janke, Kathleen A Burke, Shannon N Rhoads, Gül H Zerze, Robert O'Meally, Gregory L Dignon, Alexander E Conicella, Wenwei Zheng, Robert B Best, Robert N Cole, Jeetain Mittal, Frank Shewmaker, Nicolas L Fawzi
Neuronal inclusions of aggregated RNA-binding protein fused in sarcoma (FUS) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's nearly uncharged, aggregation-prone, yeast prion-like, low sequence-complexity domain (LC) is known to be targeted for phosphorylation. Here we map in vitro and in-cell phosphorylation sites across FUS LC We show that both phosphorylation and phosphomimetic variants reduce its aggregation-prone/prion-like character, disrupting FUS phase separation in the presence of RNA or salt and reducing FUS propensity to aggregate...
August 8, 2017: EMBO Journal
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