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Journal articles on the topic 'Prions'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Bostock, Chris. "Prions prions prions." Virus Research 48, no. 1 (1997): 107–8. http://dx.doi.org/10.1016/s0168-1702(96)01414-1.

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2

Livingston, K. "More on Prions: Prions Prions Prions." Science 273, no. 5278 (1996): 1053a. http://dx.doi.org/10.1126/science.273.5278.1053a.

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3

Obi, R. K., and F. C. Nwanebu. "Prions And Prion Diseases." African Journal of Clinical and Experimental Microbiology 9, no. 1 (2008): 38. http://dx.doi.org/10.4314/ajcem.v9i1.7481.

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4

Beekes, Michael. "Prions and prion diseases." FEBS Journal 274, no. 3 (2007): 575. http://dx.doi.org/10.1111/j.1742-4658.2006.05629.x.

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5

Wickner, R. B., K. L. Taylor, H. K. Edskes, and M.-L. Maddelein. "Prions: Portable prion domains." Current Biology 10, no. 9 (2000): R335—R337. http://dx.doi.org/10.1016/s0960-9822(00)00460-7.

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6

Nixon, Randal R. "Prions and Prion Diseases." Laboratory Medicine 30, no. 5 (1999): 335–38. http://dx.doi.org/10.1093/labmed/30.5.335.

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7

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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8

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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9

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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10

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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11

Gambetti, P. "Approaches to Prions: Prion Diseases." Science 273, no. 5278 (1996): 1052b—1053b. http://dx.doi.org/10.1126/science.273.5278.1052b.

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12

Stahl, Neil, and Stanley B. Prusiner. "Prions and prion proteins 1." FASEB Journal 5, no. 13 (1991): 2799–807. http://dx.doi.org/10.1096/fasebj.5.13.1916104.

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13

Fraser, Paul E. "Prions and Prion-like Proteins." Journal of Biological Chemistry 289, no. 29 (2014): 19839–40. http://dx.doi.org/10.1074/jbc.r114.583492.

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14

Fisher, Elizabeth, Glenn Telling, and John Collinge. "Prions and the prion disorders." Mammalian Genome 9, no. 7 (1998): 497–502. http://dx.doi.org/10.1007/s003359900807.

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15

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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16

Jones, Rachel. "Prions, prions everywhere." Nature Reviews Neuroscience 4, no. 1 (2003): 11. http://dx.doi.org/10.1038/nrn1020.

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17

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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18

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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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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20

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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21

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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22

Bodemer, Walter. "Prions." Primate Biology 3, no. 2 (2016): 47–50. http://dx.doi.org/10.5194/pb-3-47-2016.

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Abstract. Prions gained widespread public and scientific interest in the year 2000. At that time, the human neurological Creutzfeldt–Jakob disease (CJD) was known. However, new CJD cases were diagnosed but they could not be ascribed to one of the classical CJD categories i.e. sporadic (sCJD), hereditary or acquired. Hence, they were classified as variant CJD (vCJD). Later on, experimental evidence suggested that vCJD was caused by prions postulated as unique novel infectious agents and, for example, responsible for bovine spongiform encephalopathy (BSE) also known as mad cow disease. The infec

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23

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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24

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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25

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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26

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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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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28

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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Malato, Laurent, and Sven J. Saupe. "Fungal prions: When proteins turn into genes." Biochemist 27, no. 4 (2005): 14–18. http://dx.doi.org/10.1042/bio02704014.

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Prions are infectious proteic particles devoid of nucleic acids that can cause devastating neurological disorders in mammals. Prions have also been identified in simpler organisms, namely unicellular yeasts and filamentous fungi. These fungal prions represent valuable model systems because they are safe to handle and, compared with mammalian prions, easier to study. In this article, we summarize the basic characteristics of the fungal prions and attempt to describe how their discovery has affected and expanded the prion concept.

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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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Mathiason, Candace K. "Silent Prions and Covert Prion Transmission." PLOS Pathogens 11, no. 12 (2015): e1005249. http://dx.doi.org/10.1371/journal.ppat.1005249.

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32

Ridler, Charlotte. "'Anti-prions' block prion disease onset." Nature Reviews Neurology 13, no. 9 (2017): 514. http://dx.doi.org/10.1038/nrneurol.2017.100.

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33

Gilch, Sabine, and Hermann M. Schätzl. "Aptamers against prion proteins and prions." Cellular and Molecular Life Sciences 66, no. 15 (2009): 2445–55. http://dx.doi.org/10.1007/s00018-009-0031-5.

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34

Belay, Ermias D. "Prions and Prion Diseases: Current Perspectives." Emerging Infectious Diseases 10, no. 12 (2004): 2265–66. http://dx.doi.org/10.3201/eid1012.3040847.

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35

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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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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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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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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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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Kobayashi, Atsushi, Nobuyuki Sakuma, Yuichi Matsuura, Shirou Mohri, Adriano Aguzzi, and Tetsuyuki Kitamoto. "Experimental Verification of a Traceback Phenomenon in Prion Infection." Journal of Virology 84, no. 7 (2010): 3230–38. http://dx.doi.org/10.1128/jvi.02387-09.

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ABSTRACT The clinicopathological phenotypes of sporadic Creutzfeldt-Jakob disease (sCJD) correlate with the allelotypes (M or V) of the polymorphic codon 129 of the human prion protein (PrP) gene and the electrophoretic mobility patterns of abnormal prion protein (PrPSc). Transmission of sCJD prions to mice expressing human PrP with a heterologous genotype (referred to as cross-sequence transmission) results in prolonged incubation periods. We previously reported that cross-sequence transmission can generate a new prion strain with unique transmissibility, designated a traceback phenomenon. To

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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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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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Block, Alyssa J., Ronald A. Shikiya, Thomas E. Eckland, et al. "Efficient interspecies transmission of synthetic prions." PLOS Pathogens 17, no. 7 (2021): e1009765. http://dx.doi.org/10.1371/journal.ppat.1009765.

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Prions are comprised solely of PrPSc, the misfolded self-propagating conformation of the cellular protein, PrPC. Synthetic prions are generated in vitro from minimal components and cause bona fide prion disease in animals. It is unknown, however, if synthetic prions can cross the species barrier following interspecies transmission. To investigate this, we inoculated Syrian hamsters with murine synthetic prions. We found that all the animals inoculated with murine synthetic prions developed prion disease characterized by a striking uniformity of clinical onset and signs of disease. Serial intra

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Schmidt, Christian, Jeremie Fizet, Francesca Properzi, et al. "A systematic investigation of production of synthetic prions from recombinant prion protein." Open Biology 5, no. 12 (2015): 150165. http://dx.doi.org/10.1098/rsob.150165.

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According to the protein-only hypothesis, infectious mammalian prions, which exist as distinct strains with discrete biological properties, consist of multichain assemblies of misfolded cellular prion protein (PrP). A critical test would be to produce prion strains synthetically from defined components. Crucially, high-titre ‘synthetic' prions could then be used to determine the structural basis of infectivity and strain diversity at the atomic level. While there have been multiple reports of production of prions from bacterially expressed recombinant PrP using various methods, systematic prod

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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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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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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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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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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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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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