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Journal articles on the topic 'Prione'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Sedoshkina, K., E. Drozdova, S. Nikolayeva, and E. Rystsova. "Prion diseases animals." Bulletin of Science and Practice, no. 4 (April 14, 2017): 61–66. https://doi.org/10.5281/zenodo.546285.

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Priones are an absolutely new class of infectious agents, which basically differs from protozoa, bacterium’s, fungus and viral agents. They can evoke genetic, infectious and sporadic diseases with obligatory disturbance of the brain. The conversion of prione protein because of nature structure disturbance is the fundamental reason for a display of pathogenicity this protein.

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2

Bian, Jifeng, Vadim Khaychuk, Rachel C. Angers, et al. "Prion replication without host adaptation during interspecies transmissions." Proceedings of the National Academy of Sciences 114, no. 5 (2017): 1141–46. http://dx.doi.org/10.1073/pnas.1611891114.

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Adaptation of prions to new species is thought to reflect the capacity of the host-encoded cellular form of the prion protein (PrPC) to selectively propagate optimized prion conformations from larger ensembles generated in the species of origin. Here we describe an alternate replicative process, termed nonadaptive prion amplification (NAPA), in which dominant conformers bypass this requirement during particular interspecies transmissions. To model susceptibility of horses to prions, we produced transgenic (Tg) mice expressing cognate PrPC. Although disease transmission to only a subset of infe

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3

Son, Moonil, and Reed B. Wickner. "Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry." Viruses 14, no. 9 (2022): 1945. http://dx.doi.org/10.3390/v14091945.

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Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein. These prions arise spontaneously in the cell without known reason, and their effects were generally considered to be fatal based on prion diseases in humans or mammals. However, the wide array of prion studies in yeast including filamentous fungi revealed that their effects can range widely, from lethal to very mild (even cryptic) or functional, depending on the nature of the prion protein and the specific prion variant (

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4

Watts, Joel C., Kurt Giles, Daniel J. Saltzberg, et al. "Guinea Pig Prion Protein Supports Rapid Propagation of Bovine Spongiform Encephalopathy and Variant Creutzfeldt-Jakob Disease Prions." Journal of Virology 90, no. 21 (2016): 9558–69. http://dx.doi.org/10.1128/jvi.01106-16.

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ABSTRACTThe biochemical and neuropathological properties of bovine spongiform encephalopathy (BSE) and variant Creutzfeldt-Jakob disease (vCJD) prions are faithfully maintained upon transmission to guinea pigs. However, primary and secondary transmissions of BSE and vCJD in guinea pigs result in long incubation periods of ∼450 and ∼350 days, respectively. To determine if the incubation periods of BSE and vCJD prions could be shortened, we generated transgenic (Tg) mice expressing guinea pig prion protein (GPPrP). Inoculation of Tg(GPPrP) mice with BSE and vCJD prions resulted in mean incubatio

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5

Miller, Sarah C., Andrea K. Wegrzynowicz, Sierra J. Cole, Rachel E. Hayward, Samantha J. Ganser, and Justin K. Hines. "Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions." Viruses 14, no. 10 (2022): 2160. http://dx.doi.org/10.3390/v14102160.

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Yeast prions are protein-based transmissible elements, most of which are amyloids. The chaperone protein network in yeast is inexorably linked to the spreading of prions during cell division by fragmentation of amyloid prion aggregates. Specifically, the core “prion fragmentation machinery” includes the proteins Hsp104, Hsp70 and the Hsp40/J-domain protein (JDP) Sis1. Numerous novel amyloid-forming proteins have been created and examined in the yeast system and occasionally these amyloids are also capable of continuous Hsp104-dependent propagation in cell populations, forming synthetic prions.

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6

Pritzkow, Sandra, Isaac Schauer, Ananya Tupaki-Sreepurna, Rodrigo Morales, and Claudio Soto. "Screening of Anti-Prion Compounds Using the Protein Misfolding Cyclic Amplification Technology." Biomolecules 14, no. 9 (2024): 1113. http://dx.doi.org/10.3390/biom14091113.

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Prion diseases are 100% fatal infectious neurodegenerative diseases affecting the brains of humans and other mammals. The disease is caused by the formation and replication of prions, composed exclusively of the misfolded prion protein (PrPSc). We invented and developed the protein misfolding cyclic amplification (PMCA) technology for in vitro prion replication, which allow us to replicate the infectious agent and it is commonly used for ultra-sensitive prion detection in biological fluids, tissues and environmental samples. In this article, we studied whether PMCA can be used to screen for ch

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7

Walsh, Daniel J., Judy R. Rees, Surabhi Mehra, et al. "Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease." PLOS Pathogens 20, no. 4 (2024): e1012087. http://dx.doi.org/10.1371/journal.ppat.1012087.

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Prion diseases uniquely manifest in three distinct forms: inherited, sporadic, and infectious. Wild-type prions are responsible for the sporadic and infectious versions, while mutant prions cause inherited variants like fatal familial insomnia (FFI) and familial Creutzfeldt-Jakob disease (fCJD). Although some drugs can prolong prion incubation times up to four-fold in rodent models of infectious prion diseases, no effective treatments for FFI and fCJD have been found. In this study, we evaluated the efficacy of various anti-prion drugs on newly-developed knock-in mouse models for FFI and fCJD.

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8

Krauss, Sybille, and Ina Vorberg. "PrionsEx Vivo: What Cell Culture Models Tell Us about Infectious Proteins." International Journal of Cell Biology 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/704546.

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Prions are unconventional infectious agents that are composed of misfolded aggregated prion protein. Prions replicate their conformation by template-assisted conversion of the endogenous prion protein PrP. Templated conversion of soluble proteins into protein aggregates is also a hallmark of other neurodegenerative diseases. Alzheimer’s disease or Parkinson’s disease are not considered infectious diseases, although aggregate pathology appears to progress in a stereotypical fashion reminiscent of the spreading behavior ofmammalian prions. While basic principles of prion formation have been stud

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9

Krejciova, Zuzana, James Alibhai, Chen Zhao, et al. "Human stem cell–derived astrocytes replicate human prions in a PRNP genotype–dependent manner." Journal of Experimental Medicine 214, no. 12 (2017): 3481–95. http://dx.doi.org/10.1084/jem.20161547.

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Prions are infectious agents that cause neurodegenerative diseases such as Creutzfeldt–Jakob disease (CJD). The absence of a human cell culture model that replicates human prions has hampered prion disease research for decades. In this paper, we show that astrocytes derived from human induced pluripotent stem cells (iPSCs) support the replication of prions from brain samples of CJD patients. For experimental exposure of astrocytes to variant CJD (vCJD), the kinetics of prion replication occur in a prion protein codon 129 genotype–dependent manner, reflecting the genotype-dependent susceptibili

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10

Ho, Nancy, Reece McGinn, Paulina Soto, et al. "Distribution of chronic wasting disease (CWD) prions in tissues from experimentally exposed coyotes (Canis latrans)." PLOS One 20, no. 7 (2025): e0327485. https://doi.org/10.1371/journal.pone.0327485.

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Cervids susceptible to chronic wasting disease (CWD) are sympatric with multiple other animal species that can interact with infectious prions. Several reports have described the susceptibility of other species to CWD prions, or their potential to transport them. One of these species is the coyote (Canis latrans), which has been previously shown to pass transmission-relevant prion titers in their feces for at least three days after ingesting prion-positive brain material. The current study followed up on these findings and evaluated the distribution of prions in multiple tissues from the same

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Tahir, Waqas, Basant Abdulrahman, Dalia H. Abdelaziz, Simrika Thapa, Rupali Walia, and Hermann M. Schätzl. "An astrocyte cell line that differentially propagates murine prions." Journal of Biological Chemistry 295, no. 33 (2020): 11572–83. http://dx.doi.org/10.1074/jbc.ra120.012596.

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Prion diseases are fatal infectious neurodegenerative disorders in human and animals caused by misfolding of the cellular prion protein (PrPC) into the pathological isoform PrPSc. Elucidating the molecular and cellular mechanisms underlying prion propagation may help to develop disease interventions. Cell culture systems for prion propagation have greatly advanced molecular insights into prion biology, but translation of in vitro to in vivo findings is often disappointing. A wider range of cell culture systems might help overcome these shortcomings. Here, we describe an immortalized mouse neur

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12

Baune, Chase, Bradley R. Groveman, Andrew G. Hughson, et al. "Efficacy of Wex-cide 128 disinfectant against multiple prion strains." PLOS ONE 18, no. 8 (2023): e0290325. http://dx.doi.org/10.1371/journal.pone.0290325.

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Prion diseases are transmissible, fatal neurologic diseases that include Creutzfeldt-Jakob Disease (CJD) in humans, chronic wasting disease (CWD) in cervids, bovine spongiform encephalopathy (BSE) in cattle and scrapie in sheep. Prions are extremely difficult to inactivate and established methods to reduce prion infectivity are often dangerous, caustic, expensive, or impractical. Identifying viable and safe methods for treating prion contaminated materials is important for hospitals, research facilities, biologists, hunters, and meat-processors. For three decades, some prion researchers have u

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Safar, Jiri G., Klaus Kellings, Ana Serban, et al. "Search for a Prion-Specific Nucleic Acid." Journal of Virology 79, no. 16 (2005): 10796–806. http://dx.doi.org/10.1128/jvi.79.16.10796-10806.2005.

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ABSTRACT Diversity of prion strains was attributed to an elusive nucleic acid, yet a search spanning nearly two decades has failed to identify a prion-specific polynucleotide. In our search for a prion-specific nucleic acid, we analyzed nucleic acids in purified fractions from the brains of Syrian hamsters infected with Sc237 prions. Purification of Sc237 prions removed nucleic acids larger than 50 nucleotides as measured by return refocusing electrophoresis (RRGE). To determine the size of the largest polynucleotide present in purified fractions at an abundance of one molecule per infectious

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14

Evarts, Jacob, and Mikala Capage. "Hunting for Prions: Propagating Putative Prion States in Budding Yeast." Oregon Undergraduate Research Journal 18, no. 1 (2021): 26–34. http://dx.doi.org/10.5399/uo/ourj/18.1.4.

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Prions have been closely associated with fatal neurodegenerative diseases. Recent evidence, however, suggests that prions also represent an additional class of epigenetic mechanism that is biologically beneficial. From an evolutionary standpoint, the ability to change phenotypes without requiring changes to the genome, as prions do, would be hugely beneficial in fluctuating environments. Through overexpressing proteins and introducing environmental stressors, two techniques known to increase de novo prion formation, we performed a large-scale screen of many RNA-modifying enzymes in budding yea

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15

Terry, Cassandra, Adam Wenborn, Nathalie Gros, et al. "Ex vivo mammalian prions are formed of paired double helical prion protein fibrils." Open Biology 6, no. 5 (2016): 160035. http://dx.doi.org/10.1098/rsob.160035.

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Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained obscure. Recently, we developed novel methods to obtain exceptionally pure preparations of prions from mouse brain and showed that pathogenic PrP in these high-titre preparations is assembled into rod-like assemblies. Here, we have used precise cell culture-based prion infectivity assays to define the physical relationship between the PrP rods and pr

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16

Zhouravleva, Galina A., Stanislav A. Bondarev, and Nina P. Trubitsina. "How Big Is the Yeast Prion Universe?" International Journal of Molecular Sciences 24, no. 14 (2023): 11651. http://dx.doi.org/10.3390/ijms241411651.

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The number of yeast prions and prion-like proteins described since 1994 has grown from two to nearly twenty. If in the early years most scientists working with the classic mammalian prion, PrPSc, were skeptical about the possibility of using the term prion to refer to yeast cytoplasmic elements with unusual properties, it is now clear that prion-like phenomena are widespread and that yeast can serve as a convenient model for studying them. Here we give a brief overview of the yeast prions discovered so far and focus our attention to the various approaches used to identify them. The prospects f

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17

Groveman, Bradley R., Brent Race, Andrew G. Hughson, and Cathryn L. Haigh. "Sodium hypochlorite inactivation of human CJD prions." PLOS ONE 19, no. 11 (2024): e0312837. http://dx.doi.org/10.1371/journal.pone.0312837.

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Prion diseases are transmissible, fatal neurologic diseases of mammals caused by the accumulation of mis-folded, disease associated prion protein (PrPd). Creutzfeldt-Jakob Disease (CJD) is the most common human prion disease and can occur by sporadic onset (sCJD) (~85% of CJD cases), genetic mutations in the prion protein gene (10–15%) or iatrogenic transmission (rare). PrPd is difficult to inactivate and many methods to reduce prion infectivity are dangerous, caustic, expensive, or impractical. Identifying viable and safe methods for decontamination of CJD exposed materials is critically impo

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Uchiyama, Keiji, Hideyuki Hara, Junji Chida, et al. "Ethanolamine Is a New Anti-Prion Compound." International Journal of Molecular Sciences 22, no. 21 (2021): 11742. http://dx.doi.org/10.3390/ijms222111742.

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Prion diseases are a group of fatal neurodegenerative disorders caused by accumulation of proteinaceous infectious particles, or prions, which mainly consist of the abnormally folded, amyloidogenic prion protein, designated PrPSc. PrPSc is produced through conformational conversion of the cellular isoform of prion protein, PrPC, in the brain. To date, no effective therapies for prion diseases have been developed. In this study, we incidentally noticed that mouse neuroblastoma N2a cells persistently infected with 22L scrapie prions, termed N2aC24L1-3 cells, reduced PrPSc levels when cultured in

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Groener, Albrecht, Wolfram Schäfer, Henry Baron, and Martin Vey. "Hamster Prions Are a Suitable Model for Partitioning of Human CJD Prions during Plasma Processing Steps." Blood 104, no. 11 (2004): 3644. http://dx.doi.org/10.1182/blood.v104.11.3644.3644.

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Abstract Prion removal evaluation of plasma processing procedures is one important basis to assess the margin of safety of plasma protein therapeutics. Currently, in these evaluation studies to assess the removal capacity of selected manufacturing steps for human prions mainly prions derived from scrapie-infected hamsters or mice are used in spiking studies. In order to test the validity of hamster prions instead of different human prion strains as spiking reagents, we compared the partitioning of these prion preparations at two purification steps common to the manufacturing of several human p

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Barbitoff, Yury A., Andrew G. Matveenko, and Galina A. Zhouravleva. "Differential Interactions of Molecular Chaperones and Yeast Prions." Journal of Fungi 8, no. 2 (2022): 122. http://dx.doi.org/10.3390/jof8020122.

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Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction between the protein quality control (PQC) machinery and misfolded proteins. More than ten prions have been identified in yeast, of which the most studied ones include [PSI+], [URE3], and [PIN+]. While all of the major molecular chaperones have been implicated in propagation of yeast prions, many of these chaperones differentially impact propagat

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Jheeta, Sohan, Elias Chatzitheodoridis, Kevin Devine, and Janice Block. "The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis." Life 11, no. 9 (2021): 872. http://dx.doi.org/10.3390/life11090872.

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In this paper the hypothesis that prions and prion-like molecules could have initiated the chemical evolutionary process which led to the eventual emergence of life is reappraised. The prions first hypothesis is a specific application of the protein-first hypothesis which asserts that protein-based chemical evolution preceded the evolution of genetic encoding processes. This genetics-first hypothesis asserts that an “RNA-world era” came before protein-based chemical evolution and rests on a singular premise that molecules such as RNA, acetyl-CoA, and NAD are relics of a long line of chemical e

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Mathur, Vidhu, Vibha Taneja, Yidi Sun, and Susan W. Liebman. "Analyzing the Birth and Propagation of Two Distinct Prions, [PSI+] and [Het-s]y, in Yeast." Molecular Biology of the Cell 21, no. 9 (2010): 1449–61. http://dx.doi.org/10.1091/mbc.e09-11-0927.

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Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin protein (with expanded polyQ), depend on a Gln or Asn (QN)-rich region for amyloid formation. Other prions, e.g., mammalian PrP and the [Het-s] prion of Podospora anserina, although still able to form infectious amyloid aggregates, do not have QN-rich regions. Furthermore, [Het-s] and yeast prions appear to differ dramatically in their amyloid conformation. Despite these differences, a fusion of the Het-s prion domain to GFP (Het-sPrD-GFP) can propagate in yeast as a prion called [Het-s]y. We analyzed the

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Jack, Kezia, Graham S. Jackson, and Jan Bieschke. "Essential Components of Synthetic Infectious Prion Formation De Novo." Biomolecules 12, no. 11 (2022): 1694. http://dx.doi.org/10.3390/biom12111694.

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Prion diseases are a class of neurodegenerative diseases that are uniquely infectious. Whilst their general replication mechanism is well understood, the components required for the formation and propagation of highly infectious prions are poorly characterized. The protein-only hypothesis posits that the prion protein (PrP) is the only component of the prion; however, additional co-factors are required for its assembly into infectious prions. These can be provided by brain homogenate, but synthetic lipids and non-coding RNA have also been used in vitro. Here, we review a range of experimental

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Heinzer, Daniel, Merve Avar, Manuela Pfammatter, et al. "Advancing surgical instrument safety: A screen of oxidative and alkaline prion decontaminants using real-time quaking-induced conversion with prion-coated steel beads as surgical instrument mimetic." PLOS ONE 19, no. 6 (2024): e0304603. http://dx.doi.org/10.1371/journal.pone.0304603.

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Iatrogenic transmission of prions, the infectious agents of fatal Creutzfeldt-Jakob disease, through inefficiently decontaminated medical instruments remains a critical issue. Harsh chemical treatments are effective, but not suited for routine reprocessing of reusable surgical instruments in medical cleaning and disinfection processes due to material incompatibilities. The identification of mild detergents with activity against prions is therefore of high interest but laborious due to the low throughput of traditional assays measuring prion infectivity. Here, we report the establishment of TES

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Vorberg, Ina M. "All the Same? The Secret Life of Prion Strains within Their Target Cells." Viruses 11, no. 4 (2019): 334. http://dx.doi.org/10.3390/v11040334.

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Prions are infectious β-sheet-rich protein aggregates composed of misfolded prion protein (PrPSc) that do not possess coding nucleic acid. Prions replicate by recruiting and converting normal cellular PrPC into infectious isoforms. In the same host species, prion strains target distinct brain regions and cause different disease phenotypes. Prion strains are associated with biophysically distinct PrPSc conformers, suggesting that strain properties are enciphered within alternative PrPSc quaternary structures. So far it is unknown how prion strains target specific cells and initiate productive i

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Wälzlein, Joo-Hee, Karla A. Schwenke, and Michael Beekes. "Propagation of CJD Prions in Primary Murine Glia Cells Expressing Human PrPc." Pathogens 10, no. 8 (2021): 1060. http://dx.doi.org/10.3390/pathogens10081060.

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There are various existing cell models for the propagation of animal prions. However, in vitro propagation of human prions has been a long-standing challenge. This study presents the establishment of a long-term primary murine glia culture expressing the human prion protein homozygous for methionine at codon 129, which allows in vitro propagation of Creutzfeldt–Jakob disease (CJD) prions (variant CJD (vCJD) and sporadic CJD (sCJD) type MM2). Prion propagation could be detected by Western blotting of pathological proteinase K-resistant prion protein (PrPSc) from 120 days post exposure. The accu

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Benilova, Iryna, Madeleine Reilly, Cassandra Terry, et al. "Highly infectious prions are not directly neurotoxic." Proceedings of the National Academy of Sciences 117, no. 38 (2020): 23815–22. http://dx.doi.org/10.1073/pnas.2007406117.

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Prions are infectious agents which cause rapidly lethal neurodegenerative diseases in humans and animals following long, clinically silent incubation periods. They are composed of multichain assemblies of misfolded cellular prion protein. While it has long been assumed that prions are themselves neurotoxic, recent development of methods to obtain exceptionally pure prions from mouse brain with maintained strain characteristics, and in which defined structures—paired rod-like double helical fibers—can be definitively correlated with infectivity, allowed a direct test of this assertion. Here we

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Poddar, Anirban, T. N. Kundu, Manaly Sinha Ray, and Rituparna Maji. "Transmissible Spongiform Encephalopathies Prion Proteins: A Systematic Review." International Journal of Applied Biology 7, no. 2 (2023): 46–53. http://dx.doi.org/10.20956/ijab.v7i2.31044.

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Prion proteins (PrPc) have been implicated as the causative agent of “Transmissible Spongiform Encephalopathies” (TSE). Apart from this devilish role, prions also have a bright facet of their own and their identity holds much more than just being a pathogenic entity. Role of prions as scaffolding proteins for ligand binding and signal transduction has been reported by several researchers. Role of prions in nerve impulse transmission at neuronal junctions, glyapse and gap junctions have been reported. Prion mediated regulation of calcium ion flux and redox status in turn regulates many major ce

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Peretz, David, Surachai Supattapone, Kurt Giles, et al. "Inactivation of Prions by Acidic Sodium Dodecyl Sulfate." Journal of Virology 80, no. 1 (2006): 322–31. http://dx.doi.org/10.1128/jvi.80.1.322-331.2006.

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ABSTRACT Prompted by the discovery that prions become protease-sensitive after exposure to branched polyamine dendrimers in acetic acid (AcOH) (S. Supattapone, H. Wille, L. Uyechi, J. Safar, P. Tremblay, F. C. Szoka, F. E. Cohen, S. B. Prusiner, and M. R. Scott, J. Virol. 75:3453-3461, 2001), we investigated the inactivation of prions by sodium dodecyl sulfate (SDS) in weak acid. As judged by sensitivity to proteolytic digestion, the disease-causing prion protein (PrPSc) was denatured at room temperature by SDS at pH values of ≤4.5 or ≥10. Exposure of Sc237 prions in Syrian hamster brain homog

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Wickner, Reed B., Herman K. Edskes, Moonil Son, and Songsong Wu. "Anti-Prion Systems Block Prion Transmission, Attenuate Prion Generation, Cure Most Prions as They Arise and Limit Prion-Induced Pathology in Saccharomyces cerevisiae." Biology 11, no. 9 (2022): 1266. http://dx.doi.org/10.3390/biology11091266.

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All variants of the yeast prions [PSI+] and [URE3] are detrimental to their hosts, as shown by the dramatic slowing of growth (or even lethality) of a majority, by the rare occurrence in wild isolates of even the mildest variants and by the absence of reproducible benefits of these prions. To deal with the prion problem, the host has evolved an array of anti-prion systems, acting in normal cells (without overproduction or deficiency of any component) to block prion transmission from other cells, to lower the rates of spontaneous prion generation, to cure most prions as they arise and to limit

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Wickner, Reed, Moonil Son, and Herman Edskes. "Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems." Viruses 11, no. 3 (2019): 238. http://dx.doi.org/10.3390/v11030238.

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The known amyloid-based prions of Saccharomyces cerevisiae each have multiple heritable forms, called “prion variants” or “prion strains”. These variants, all based on the same prion protein sequence, differ in their biological properties and their detailed amyloid structures, although each of the few examined to date have an in-register parallel folded β sheet architecture. Here, we review the range of biological properties of yeast prion variants, factors affecting their generation and propagation, the interaction of prion variants with each other, the mutability of prions, and their segrega

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Thapa, Simrika, Cristobal Marrero Winkens, Waqas Tahir, Maria I. Arifin, Sabine Gilch, and Hermann M. Schatzl. "Gene-Edited Cell Models to Study Chronic Wasting Disease." Viruses 14, no. 3 (2022): 609. http://dx.doi.org/10.3390/v14030609.

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Prion diseases are fatal infectious neurodegenerative disorders affecting both humans and animals. They are caused by the misfolded isoform of the cellular prion protein (PrPC), PrPSc, and currently no options exist to prevent or cure prion diseases. Chronic wasting disease (CWD) in deer, elk and other cervids is considered the most contagious prion disease, with extensive shedding of infectivity into the environment. Cell culture models provide a versatile platform for convenient quantification of prions, for studying the molecular and cellular biology of prions, and for performing high-throu

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Hannaoui, Samia, Elizabeth Triscott, Camilo Duque Velásquez, et al. "New and distinct chronic wasting disease strains associated with cervid polymorphism at codon 116 of the Prnp gene." PLOS Pathogens 17, no. 7 (2021): e1009795. http://dx.doi.org/10.1371/journal.ppat.1009795.

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Chronic wasting disease (CWD) is a prion disease affecting cervids. Polymorphisms in the prion protein gene can result in extended survival of CWD-infected animals. However, the impact of polymorphisms on cellular prion protein (PrPC) and prion properties is less understood. Previously, we characterized the effects of a polymorphism at codon 116 (A>G) of the white-tailed deer (WTD) prion protein and determined that it destabilizes PrPC structure. Comparing CWD isolates from WTD expressing homozygous wild-type (116AA) or heterozygous (116AG) PrP, we found that 116AG-prions were conformationa

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Woerman, Amanda L., Jan Stöhr, Atsushi Aoyagi, et al. "Propagation of prions causing synucleinopathies in cultured cells." Proceedings of the National Academy of Sciences 112, no. 35 (2015): E4949—E4958. http://dx.doi.org/10.1073/pnas.1513426112.

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Increasingly, evidence argues that many neurodegenerative diseases, including progressive supranuclear palsy (PSP), are caused by prions, which are alternatively folded proteins undergoing self-propagation. In earlier studies, PSP prions were detected by infecting human embryonic kidney (HEK) cells expressing a tau fragment [TauRD(LM)] fused to yellow fluorescent protein (YFP). Here, we report on an improved bioassay using selective precipitation of tau prions from human PSP brain homogenates before infection of the HEK cells. Tau prions were measured by counting the number of cells with TauRD

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Bosque, Patrick J., and Stanley B. Prusiner. "Cultured Cell Sublines Highly Susceptible to Prion Infection." Journal of Virology 74, no. 9 (2000): 4377–86. http://dx.doi.org/10.1128/jvi.74.9.4377-4386.2000.

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ABSTRACT Cultured cell lines infected with prions produce an abnormal isoform of the prion protein (PrPSc). In order to derive cell lines producing sufficient quantities of PrPSc for most studies, it has been necessary to subclone infected cultures and select the subclones producing the largest amounts of PrPSc. Since postinfection cloning can introduce differences between infected and uninfected cell lines, we sought an approach to generate prion-infected cell lines that would avoid clonal artifacts. Using an improved cell blot technique, which permits sensitive and rapid comparison of PrPSc

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Barry, R. A., M. P. McKinley, P. E. Bendheim, G. K. Lewis, S. J. DeArmond, and S. B. Prusiner. "Antibodies to the scrapie protein decorate prion rods." Journal of Immunology 135, no. 1 (1985): 603–13. http://dx.doi.org/10.4049/jimmunol.135.1.603.

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Abstract Scrapie is a degenerative, transmissible neurologic disease of sheep and goats which occurs in the absence of any detectable host immune response. Antibodies to the scrapie agent have been produced after immunization of rabbits with either scrapie prions or the prion protein, PrP 27-30, purified from infected hamster brain. Immunoreactivity of the antisera was assessed by dot and Western immunoblots with purified prions and PrP 27-30. Antibodies raised against infectious prions were more immunoreactive with native than denatured preparations, whereas those raised against PrP 27-30 wer

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Kang, Hae-Eun, Youngwon Mo, Raihah Abd Rahim, Hye-Mi Lee, and Chongsuk Ryou. "Prion Diagnosis: Application of Real-Time Quaking-Induced Conversion." BioMed Research International 2017 (2017): 1–8. http://dx.doi.org/10.1155/2017/5413936.

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Prions composed of pathogenic scrapie prion protein (PrPSc) are infectious pathogens that cause progressive neurological conditions known as prion diseases or transmissible spongiform encephalopathies. Although these diseases pose considerable risk to public health, procedures for early diagnosis have not been established. One of the most recent attempts at sensitive and specific detection of prions is the real-time quaking-induced conversion (RT-QuIC) method, which measures the activity of PrPScaggregates or amyloid formation triggered by PrPScseeds in the presence of recombinant PrP. In this

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Burgener, Kate, Stuart Siegfried Lichtenberg, Daniel P. Walsh, Heather N. Inzalaco, Aaron Lomax, and Joel A. Pedersen. "Prion Seeding Activity in Plant Tissues Detected by RT-QuIC." Pathogens 13, no. 6 (2024): 452. http://dx.doi.org/10.3390/pathogens13060452.

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Prion diseases such as scrapie, bovine spongiform encephalopathy (BSE), and chronic wasting disease (CWD) affect domesticated and wild herbivorous mammals. Animals afflicted with CWD, the transmissible spongiform encephalopathy of cervids (deer, elk, and moose), shed prions into the environment, where they may persist and remain infectious for years. These environmental prions may remain in soil, be transported in surface waters, or assimilated into plants. Environmental sampling is an emerging area of TSE research and can provide more information about prion fate and transport once shed by in

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Paspaltsis, Ioannis, Eirini Kanata, Sotirios Sotiriadis, et al. "A Comparison of RML Prion Inactivation Efficiency by Heterogeneous and Homogeneous Photocatalysis." Pathogens 13, no. 5 (2024): 420. http://dx.doi.org/10.3390/pathogens13050420.

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Prions are proteinaceous pathogens responsible for a variety of devastating diseases in mammals, including scrapie in sheep and goats, chronic wasting disease in cervids, and Creutzfeldt–Jakob disease (CJD) in humans. They are characterized by their exceptional persistence to common inactivation procedures. This applies to all possible sources of prion contamination as prions may be present in the tissues and biological fluids of infected individuals. Hence, efficient prion inactivation procedures are still being sought to minimize the risk of intra- or inter-species transmission. In the past,

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Herbst, Allen, Serene Wohlgemuth, Jing Yang, et al. "Susceptibility of Beavers to Chronic Wasting Disease." Biology 11, no. 5 (2022): 667. http://dx.doi.org/10.3390/biology11050667.

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Chronic wasting disease (CWD) is a contagious, fatal, neurodegenerative prion disease of cervids. The expanding geographical range and rising prevalence of CWD are increasing the risk of pathogen transfer and spillover of CWD to non-cervid sympatric species. As beavers have close contact with environmental and food sources of CWD infectivity, we hypothesized that they may be susceptible to CWD prions. We evaluated the susceptibility of beavers to prion diseases by challenging transgenic mice expressing beaver prion protein (tgBeaver) with five strains of CWD, four isolates of rodent-adapted pr

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Herbst, Allen, Serene Wohlgemuth, Jing Yang, et al. "Susceptibility of Beavers to Chronic Wasting Disease." Biology 11, no. 5 (2022): 667. http://dx.doi.org/10.3390/biology11050667.

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Chronic wasting disease (CWD) is a contagious, fatal, neurodegenerative prion disease of cervids. The expanding geographical range and rising prevalence of CWD are increasing the risk of pathogen transfer and spillover of CWD to non-cervid sympatric species. As beavers have close contact with environmental and food sources of CWD infectivity, we hypothesized that they may be susceptible to CWD prions. We evaluated the susceptibility of beavers to prion diseases by challenging transgenic mice expressing beaver prion protein (tgBeaver) with five strains of CWD, four isolates of rodent-adapted pr

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Asante, Emmanuel A., Ian Gowland, Andrew Grimshaw, et al. "Absence of spontaneous disease and comparative prion susceptibility of transgenic mice expressing mutant human prion proteins." Journal of General Virology 90, no. 3 (2009): 546–58. http://dx.doi.org/10.1099/vir.0.007930-0.

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Approximately 15 % of human prion disease is associated with autosomal-dominant pathogenic mutations in the prion protein (PrP) gene. Previous attempts to model these diseases in mice have expressed human PrP mutations in murine PrP, but this may have different structural consequences. Here, we describe transgenic mice expressing human PrP with P102L or E200K mutations and methionine (M) at the polymorphic residue 129. Although no spontaneous disease developed in aged animals, these mice were readily susceptible to prion infection from patients with the homotypic pathogenic mutation. However,

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Arshad, Hamza, Zeel Patel, Zaid A. M. Al-Azzawi, et al. "The molecular determinants of a universal prion acceptor." PLOS Pathogens 20, no. 9 (2024): e1012538. http://dx.doi.org/10.1371/journal.ppat.1012538.

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In prion diseases, the species barrier limits the transmission of prions from one species to another. However, cross-species prion transmission is remarkably efficient in bank voles, and this phenomenon is mediated by the bank vole prion protein (BVPrP). The molecular determinants of BVPrP’s ability to function as a universal prion acceptor remain incompletely defined. Building on our finding that cultured cells expressing BVPrP can replicate both mouse and hamster prion strains, we systematically identified key residues in BVPrP that permit cross-species prion replication. We found that resid

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Tuite, Mick, Klement Stojanovski, Frederique Ness, Gloria Merritt, and Nadejda Koloteva-Levine. "Cellular factors important for the de novo formation of yeast prions." Biochemical Society Transactions 36, no. 5 (2008): 1083–87. http://dx.doi.org/10.1042/bst0361083.

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Prions represent an unusual structural form of a protein that is ‘infectious’. In mammals, prions are associated with fatal neurodegenerative diseases such as CJD (Creutzfeldt–Jakob disease), while in fungi they act as novel epigenetic regulators of phenotype. Even though most of the human prion diseases arise spontaneously, we still know remarkably little about how infectious prions form de novo. The [PSI+] prion of the yeast Saccharomyces cerevisiae provides a highly tractable model in which to explore the underlying mechanism of de novo prion formation, in particular identifying key cis- an

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Acquatella-Tran Van Ba, Isabelle, Thibaut Imberdis, and Véronique Perrier. "From Prion Diseases to Prion-Like Propagation Mechanisms of Neurodegenerative Diseases." International Journal of Cell Biology 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/975832.

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Prion diseases are fatal neurodegenerative sporadic, inherited, or acquired disorders. In humans, Creutzfeldt-Jakob disease is the most studied prion disease. In animals, the most frequent prion diseases are scrapie in sheep and goat, bovine spongiform encephalopathy in cattle, and the emerging chronic wasting disease in wild and captive deer in North America. The hallmark of prion diseases is the deposition in the brain of PrPSc, an abnormalβ-sheet-rich form of the cellular prion protein (PrPC) (Prusiner 1982). According to the prion hypothesis, PrPSccan trigger the autocatalytic conversion o

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Kushnirov, Vitaly V., Alexander A. Dergalev, Maya K. Alieva, and Alexander I. Alexandrov. "Structural Bases of Prion Variation in Yeast." International Journal of Molecular Sciences 23, no. 10 (2022): 5738. http://dx.doi.org/10.3390/ijms23105738.

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Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state aff

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Siddiqi, Mohammad Khursheed, Chae Kim, Tracy Haldiman, et al. "Structurally distinct external solvent-exposed domains drive replication of major human prions." PLOS Pathogens 17, no. 6 (2021): e1009642. http://dx.doi.org/10.1371/journal.ppat.1009642.

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There is a limited understanding of structural attributes that encode the iatrogenic transmissibility and various phenotypes of prions causing the most common human prion disease, sporadic Creutzfeldt-Jakob disease (sCJD). Here we report the detailed structural differences between major sCJD MM1, MM2, and VV2 prions determined with two complementary synchrotron hydroxyl radical footprinting techniques—mass spectrometry (MS) and conformation dependent immunoassay (CDI) with a panel of Europium-labeled antibodies. Both approaches clearly demonstrate that the phenotypically distant prions differ

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Uchiyama, Keiji, Hironori Miyata, Yoshitaka Yamaguchi, et al. "Strain-Dependent Prion Infection in Mice Expressing Prion Protein with Deletion of Central Residues 91–106." International Journal of Molecular Sciences 21, no. 19 (2020): 7260. http://dx.doi.org/10.3390/ijms21197260.

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Conformational conversion of the cellular prion protein, PrPC, into the abnormally folded isoform, PrPSc, is a key pathogenic event in prion diseases. However, the exact conversion mechanism remains largely unknown. Transgenic mice expressing PrP with a deletion of the central residues 91–106 were generated in the absence of endogenous PrPC, designated Tg(PrP∆91–106)/Prnp0/0 mice and intracerebrally inoculated with various prions. Tg(PrP∆91–106)/Prnp0/0 mice were resistant to RML, 22L and FK-1 prions, neither producing PrPSc∆91–106 or prions in the brain nor developing disease after inoculatio

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Race, Brent, Katie Phillips, Kimberly Meade-White, James Striebel, and Bruce Chesebro. "Increased Infectivity of Anchorless Mouse Scrapie Prions in Transgenic Mice Overexpressing Human Prion Protein." Journal of Virology 89, no. 11 (2015): 6022–32. http://dx.doi.org/10.1128/jvi.00362-15.

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ABSTRACTPrion protein (PrP) is found in all mammals, mostly as a glycoprotein anchored to the plasma membrane by a C-terminal glycosylphosphatidylinositol (GPI) linkage. Following prion infection, host protease-sensitive prion protein (PrPsen or PrPC) is converted into an abnormal, disease-associated, protease-resistant form (PrPres). Biochemical characteristics, such as the PrP amino acid sequence, and posttranslational modifications, such as glycosylation and GPI anchoring, can affect the transmissibility of prions as well as the biochemical properties of the PrPres generated. Previousin viv

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Galliamov, Arthur A., Valery N. Urakov, Alexander A. Dergalev, and Vitaly V. Kushnirov. "On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins." International Journal of Molecular Sciences 26, no. 4 (2025): 1637. https://doi.org/10.3390/ijms26041637.

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The prion-forming regions (PFRs) of yeast prion proteins are usually located at either the N- or C-terminus of a protein. In the Sup35 prion, the main prion structure contains 71 N-terminal residues. Here, we investigated the importance of the terminal PFR location for prion properties. Two prionogenic sequences of 29 and 30 residues and two random sequences of 23 and 15 residues were added to the Sup35 N-terminus, making the original PFR internal. These proteins were overproduced in yeast with two variants of the Sup35 prion. Mapping of the prion-like structures of these proteins by partial p

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