Journal articles: 'Prion protein'

1

Requena, Jesús R. "The protean prion protein." PLOS Biology 18, no. 6 (June 25, 2020): e3000754. http://dx.doi.org/10.1371/journal.pbio.3000754.

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Ma, Jiyan, Jingjing Zhang, and Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers." Viruses 14, no. 9 (August 31, 2022): 1940. http://dx.doi.org/10.3390/v14091940.

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Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. Over the years, a plethora of misfolded recPrP conformers have been generated, but despite their seeding capability, many of them have failed to elicit a fatal neurodegenerative disorder in wild-type animals like a naturally occurring prion. The application of the protein misfolding cyclic amplification technique and the inclusion of non-protein cofactors in the reaction mixture have led to the generation of authentic recombinant prions that fully recapitulate the characteristics of native prions. Together, these studies reveal that recPrP can stably exist in a variety of misfolded conformations and when inoculated into wild-type animals, misfolded recPrP conformers cause a wide range of outcomes, from being completely innocuous to lethal. Since all these recPrP conformers possess seeding capabilities, these results clearly suggest that seeding activity alone is not equivalent to prion activity. Instead, authentic prions are those PrP conformers that are not only heritable (the ability to seed the conversion of normal PrP) but also pathogenic (the ability to cause fatal neurodegeneration). The knowledge gained from the studies of the recombinant prion is important for us to understand the pathogenesis of prion disease and the roles of misfolded proteins in other neurodegenerative disorders.

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Atkinson, Caroline J., Kai Zhang, Alan L. Munn, Adrian Wiegmans, and Ming Q. Wei. "Prion protein scrapie and the normal cellular prion protein." Prion 10, no. 1 (December 8, 2015): 63–82. http://dx.doi.org/10.1080/19336896.2015.1110293.

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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 (September 1, 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 (or strain) made by the same prion protein but with a different conformation. This prion biology is affected by an array of molecular chaperone systems, such as Hsp40, Hsp70, Hsp104, and combinations of them. In parallel with the systems required for prion propagation, yeast has multiple anti-prion systems, constantly working in the normal cell without overproduction of or a deficiency in any protein, which have negative effects on prions by blocking their formation, curing many prions after they arise, preventing prion infections, and reducing the cytotoxicity produced by prions. From the protectors of nascent polypeptides (Ssb1/2p, Zuo1p, and Ssz1p) to the protein sequesterase (Btn2p), the disaggregator (Hsp104), and the mysterious Cur1p, normal levels of each can cure the prion variants arising in its absence. The controllers of mRNA quality, nonsense-mediated mRNA decay proteins (Upf1, 2, 3), can cure newly formed prion variants by association with a prion-forming protein. The regulator of the inositol pyrophosphate metabolic pathway (Siw14p) cures certain prion variants by lowering the levels of certain organic compounds. Some of these proteins have other cellular functions (e.g., Btn2), while others produce an anti-prion effect through their primary role in the normal cell (e.g., ribosomal chaperones). Thus, these anti-prion actions are the innate defense strategy against prions. Here, we outline the anti-prion systems in yeast that produce innate immunity to prions by a multi-layered operation targeting each step of prion development.

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Dimcheff, Derek E., John L. Portis, and Byron Caughey. "Prion proteins meet protein quality control." Trends in Cell Biology 13, no. 7 (July 2003): 337–40. http://dx.doi.org/10.1016/s0962-8924(03)00125-9.

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6

Kupfer, L., W. Hinrichs, and M. Groschup. "Prion Protein Misfolding." Current Molecular Medicine 9, no. 7 (September 1, 2009): 826–35. http://dx.doi.org/10.2174/156652409789105543.

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7

Rezaei, H. "Prion Protein Oligomerization." Current Alzheimer Research 5, no. 6 (December 1, 2008): 572–78. http://dx.doi.org/10.2174/156720508786898497.

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Lawson, Victoria A., Steven J. Collins, Colin L. Masters, and Andrew F. Hill. "Prion protein glycosylation." Journal of Neurochemistry 93, no. 4 (May 2005): 793–801. http://dx.doi.org/10.1111/j.1471-4159.2005.03104.x.

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9

Gough, N. R. "Prion Protein Protection." Science Signaling 1, no. 19 (May 13, 2008): ec174-ec174. http://dx.doi.org/10.1126/stke.119ec174.

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10

Prusiner, Stanley B., Michael R. Scott, Stephen J. DeArmond, and Fred E. Cohen. "Prion Protein Biology." Cell 93, no. 3 (May 1998): 337–48. http://dx.doi.org/10.1016/s0092-8674(00)81163-0.

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11

Ghetti, Bernardino, Pedro Piccardo, Bias Frangione, Orso Bugiani, Giorgio Giaccone, Katherine Young, Frances Prelli, Martin R. Farlow, Stephen R. Dlouhy, and Fabrizio Tagliavini. "Prion Protein Amyloidosis." Brain Pathology 6, no. 2 (April 1996): 127–45. http://dx.doi.org/10.1111/j.1750-3639.1996.tb00796.x.

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12

Caughey, Byron. "Prion protein interconversions†." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 356, no. 1406 (February 28, 2001): 197–202. http://dx.doi.org/10.1098/rstb.2000.0765.

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The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use of in vitro models to describe how PrP is converted to the disease–associated, protease–resistant form. These models reflect many important biological parameters of TSE diseases and have been used to identify inhibitors of the PrP conversion as lead compounds in the development of anti–TSE drugs.

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13

Hesketh, Shirley, Andrew R. Thompsett, and David R. Brown. "Prion protein polymerisation triggered by manganese-generated prion protein seeds." Journal of Neurochemistry 120, no. 1 (November 11, 2011): 177–89. http://dx.doi.org/10.1111/j.1471-4159.2011.07540.x.

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14

Norstrom, Eric M., Mark F. Ciaccio, Benjamin Rassbach, Robert Wollmann, and James A. Mastrianni. "Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation." Journal of Virology 81, no. 6 (December 20, 2006): 2831–37. http://dx.doi.org/10.1128/jvi.02157-06.

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ABSTRACT Prion diseases are transmissible neurodegenerative diseases caused by a conformational isoform of the prion protein (PrP), a host-encoded cell surface sialoglycoprotein. Recent evidence suggests a cytosolic fraction of PrP (cyPrP) functions either as an initiating factor or toxic element of prion disease. When expressed in cultured cells, cyPrP acquires properties of the infectious conformation of PrP (PrPSc), including insolubility, protease resistance, aggregation, and toxicity. Transgenic mice (2D1 and 1D4 lines) that coexpress cyPrP and PrPC exhibit focal cerebellar atrophy, scratching behavior, and gait abnormalities suggestive of prion disease, although they lack protease-resistant PrP. To determine if the coexpression of PrPC is necessary or inhibitory to the phenotype of these mice, we crossed Tg1D4(Prnp +/+ ) mice with PrP-ablated mice (TgPrnp o/o) to generate Tg1D4(Prnp o/o) mice and followed the development of disease and pathological phenotype. We found no difference in the onset of symptoms or the clinical or pathological phenotype of disease between Tg1D4(Prnp +/+ ) and Tg1D4(Prnp o/o) mice, suggesting that cyPrP and PrPC function independently in the disease state. Additionally, Tg1D4(Prnp o/o) mice were resistant to challenge with mouse-adapted scrapie (RML), suggesting cyPrP is inaccessible to PrPSc. We conclude that disease phenotype and cellular toxicity associated with the expression of cyPrP are independent of PrPC and the generation of typical prion disease.

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15

Chakrabortee, Sohini, Can Kayatekin, Greg A. Newby, Marc L. Mendillo, Alex Lancaster, and Susan Lindquist. "Luminidependens (LD) is an Arabidopsis protein with prion behavior." Proceedings of the National Academy of Sciences 113, no. 21 (April 25, 2016): 6065–70. http://dx.doi.org/10.1073/pnas.1604478113.

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Prion proteins provide a unique mode of biochemical memory through self-perpetuating changes in protein conformation and function. They have been studied in fungi and mammals, but not yet identified in plants. Using a computational model, we identified candidate prion domains (PrDs) in nearly 500 plant proteins. Plant flowering is of particular interest with respect to biological memory, because its regulation involves remembering and integrating previously experienced environmental conditions. We investigated the prion-forming capacity of three prion candidates involved in flowering using a yeast model, where prion attributes are well defined and readily tested. In yeast, prions heritably change protein functions by templating monomers into higher-order assemblies. For most yeast prions, the capacity to convert into a prion resides in a distinct prion domain. Thus, new prion-forming domains can be identified by functional complementation of a known prion domain. The prion-like domains (PrDs) of all three of the tested proteins formed higher-order oligomers. Uniquely, the Luminidependens PrD (LDPrD) fully replaced the prion-domain functions of a well-characterized yeast prion, Sup35. Our results suggest that prion-like conformational switches are evolutionarily conserved and might function in a wide variety of normal biological processes.

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16

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 (September 30, 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. However, additional chaperone requirements, if any, have not been determined. Here, we report the first instances of a JDP-Hsp70 system requirement for the propagation of synthetic prions. We utilized constructs from a system of engineered prions with prion-forming domains (PrDs) consisting of a polyQ stretch interrupted by a single heterologous amino acid interspersed every fifth residue. These “polyQX” PrDs are fused to the MC domains of Sup35, creating chimeric proteins of which a subset forms synthetic prions in yeast. For four of these prions, we show that SIS1 repression causes prion loss in a manner consistent with Sis1′s known role in prion fragmentation. PolyQX prions were sensitive to Sis1 expression levels to differing degrees, congruent with the variability observed among native prions. Our results expand the scope known Sis1 functionality, demonstrating that Sis1 acts on amyloids broadly, rather than through specific protein–protein interactions with individual yeast prion-forming proteins.

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17

BROWN, David R. "PrPSc-like prion protein peptide inhibits the function of cellular prion protein." Biochemical Journal 352, no. 2 (November 24, 2000): 511–18. http://dx.doi.org/10.1042/bj3520511.

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Mice lacking expression of the prion protein are protected against infection with prion disease. Neurodegeneration in prion disease requires the formation of the abnormal isoform of the prion protein (PrPSc) from host prion protein. Therefore expression of normal host prion protein is necessary for prion disease. In the present investigation, it was demonstrated that PrPSc and a peptide resembling PrPSc, PrP106–126, both bind to cellular prion protein at amino acid residues 112–119. Interaction between PrP106–126 and the prion protein strips the prion protein from cells. Direct interaction of PrP106–126 with the prion protein was found to make cells more susceptible to copper toxicity, inhibited copper uptake into cells and inhibited the superoxide dismutase-like activity of the prion protein. Direct inhibition of prion protein function by PrPSc may be necessary for neurodegeneration in prion disease.

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18

Scott, Michael R. D., Darel A. Butler, Dale E. Bredesen, Monika Wälchli, Karen K. Hsiao, and Stanley B. Prusiner. "Prion protein gene expression in cultured cells." "Protein Engineering, Design and Selection" 2, no. 1 (1988): 69–76. http://dx.doi.org/10.1093/protein/2.1.69.

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19

Sakudo, Akikazu, and Kazuyoshi Ikuta. "Prion Protein Functions and Dysfunction in Prion Diseases." Current Medicinal Chemistry 16, no. 3 (January 1, 2009): 380–89. http://dx.doi.org/10.2174/092986709787002673.

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20

Zhou, Z., and G. Xiao. "Conformational conversion of prion protein in prion diseases." Acta Biochimica et Biophysica Sinica 45, no. 6 (April 11, 2013): 465–76. http://dx.doi.org/10.1093/abbs/gmt027.

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21

du Plessis, Daniel G. "Prion Protein Disease and Neuropathology of Prion Disease." Neuroimaging Clinics of North America 18, no. 1 (February 2008): 163–82. http://dx.doi.org/10.1016/j.nic.2007.12.003.

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22

Louka, Alexandra, Elsa Zacco, Piero Andrea Temussi, Gian Gaetano Tartaglia, and Annalisa Pastore. "RNA as the stone guest of protein aggregation." Nucleic Acids Research 48, no. 21 (October 17, 2020): 11880–89. http://dx.doi.org/10.1093/nar/gkaa822.

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Abstract The study of prions as infectious aggregates dates several decades. From its original formulation, the definition of a prion has progressively changed to the point that many aggregation-prone proteins are now considered bona fide prions. RNA molecules, not included in the original ‘protein-only hypothesis’, are also being recognized as important factors contributing to the ‘prion behaviour’, that implies the transmissibility of an aberrant fold. In particular, an association has recently emerged between aggregation and the assembly of prion-like proteins in RNA-rich complexes, associated with both physiological and pathological events. Here, we discuss the historical rising of the concept of prion-like domains, their relation to RNA and their role in protein aggregation. As a paradigmatic example, we present the case study of TDP-43, an RNA-binding prion-like protein associated with amyotrophic lateral sclerosis. Through this example, we demonstrate how the current definition of prions has incorporated quite different concepts making the meaning of the term richer and more stimulating. An important message that emerges from our analysis is the dual role of RNA in protein aggregation, making RNA, that has been considered for many years a ‘silent presence’ or the ‘stone guest’ of protein aggregation, an important component of the process.

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23

Das, Alvin S., and Wen-Quan Zou. "Prions: Beyond a Single Protein." Clinical Microbiology Reviews 29, no. 3 (May 25, 2016): 633–58. http://dx.doi.org/10.1128/cmr.00046-15.

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SUMMARYSince the term protein was first coined in 1838 and protein was discovered to be the essential component of fibrin and albumin, all cellular proteins were presumed to play beneficial roles in plants and mammals. However, in 1967, Griffith proposed that proteins could be infectious pathogens and postulated their involvement in scrapie, a universally fatal transmissible spongiform encephalopathy in goats and sheep. Nevertheless, this novel hypothesis had not been evidenced until 1982, when Prusiner and coworkers purified infectious particles from scrapie-infected hamster brains and demonstrated that they consisted of a specific protein that he called a “prion.” Unprecedentedly, the infectious prion pathogen is actually derived from its endogenous cellular form in the central nervous system. Unlike other infectious agents, such as bacteria, viruses, and fungi, prions do not contain genetic materials such as DNA or RNA. The unique traits and genetic information of prions are believed to be encoded within the conformational structure and posttranslational modifications of the proteins. Remarkably, prion-like behavior has been recently observed in other cellular proteins—not only in pathogenic roles but also serving physiological functions. The significance of these fascinating developments in prion biology is far beyond the scope of a single cellular protein and its related disease.

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24

Passet, Bruno, Sophie Halliez, Vincent Béringue, Hubert Laude, and Jean-Luc Vilotte. "The prion protein family." Prion 7, no. 2 (March 2013): 127–30. http://dx.doi.org/10.4161/pri.22851.

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Park, Kyung-Won, and Liming Li. "Prion protein inCaenorhabditis elegans." Prion 5, no. 1 (January 2011): 28–38. http://dx.doi.org/10.4161/pri.5.1.14026.

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26

Krakauer, David C., Mark Pagel, T. R. E. Southwood, and Paola M. de A. Zanotto. "Phylogenesis of prion protein." Nature 380, no. 6576 (April 1996): 675. http://dx.doi.org/10.1038/380675a0.

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27

Cisse, Moustapha, and Lennart Mucke. "A prion protein connection." Nature 457, no. 7233 (February 2009): 1090–91. http://dx.doi.org/10.1038/4571090a.

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28

Hammarström, Per, and Sofie Nyström. "Porcine prion protein amyloid." Prion 9, no. 4 (July 4, 2015): 266–77. http://dx.doi.org/10.1080/19336896.2015.1065373.

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29

Moser, Markus, Bruno Oesch, and Hansruedi Büeler. "An anti-prion protein?" Nature 362, no. 6417 (March 1993): 213–14. http://dx.doi.org/10.1038/362213b0.

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30

Franscini, Nicola, Ahmed El Gedaily, Ulrich Matthey, Susanne Franitza, Man-Sun Sy, Alexander Bürkle, Martin Groschup, Ueli Braun, and Ralph Zahn. "Prion Protein in Milk." PLoS ONE 1, no. 1 (December 20, 2006): e71. http://dx.doi.org/10.1371/journal.pone.0000071.

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31

Yang, Xiaowen, Yan Zhang, Lihua Zhang, Tianlin He, Jie Zhang, and Chaoyang Li. "Prion protein and cancers." Acta Biochimica et Biophysica Sinica 46, no. 6 (March 28, 2014): 431–40. http://dx.doi.org/10.1093/abbs/gmu019.

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32

Butcher, James. "Protein-only prion proposal." Lancet Neurology 3, no. 9 (September 2004): 511. http://dx.doi.org/10.1016/s1474-4422(04)00860-9.

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33

Ghetti, Bernardino, Fabrizio Tagliavini, M. Takao, Orso Bugiani, and Pedro Piccardo. "Hereditary prion protein amyloidoses." Clinics in Laboratory Medicine 23, no. 1 (March 2003): 65–85. http://dx.doi.org/10.1016/s0272-2712(02)00064-1.

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34

Rudd, P. "Glycosylation and prion protein." Current Opinion in Structural Biology 12, no. 5 (October 1, 2002): 578–86. http://dx.doi.org/10.1016/s0959-440x(02)00377-9.

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35

Zou, W. Q., and P. Gambetti. "Prion: the chameleon protein." Cellular and Molecular Life Sciences 64, no. 24 (October 29, 2007): 3266–70. http://dx.doi.org/10.1007/s00018-007-7380-8.

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36

BROWN, David R. "PrPSc-like prion protein peptide inhibits the function of cellular prion protein." Biochemical Journal 352, no. 2 (December 1, 2000): 511. http://dx.doi.org/10.1042/0264-6021:3520511.

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37

Giannopoulos, P. N., C. Robertson, J. Jodoin, H. Paudel, S. A. Booth, and A. C. LeBlanc. "Phosphorylation of Prion Protein at Serine 43 Induces Prion Protein Conformational Change." Journal of Neuroscience 29, no. 27 (July 8, 2009): 8743–51. http://dx.doi.org/10.1523/jneurosci.2294-09.2009.

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38

Thallemer, Alyssa M., Linh Bui, and Patricia Soto. "Mapping the interactions between prion protein (PrPC) and prion protein fibrils (PrPSc)." Biophysical Journal 122, no. 3 (February 2023): 468a. http://dx.doi.org/10.1016/j.bpj.2022.11.2510.

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39

Prosekov, Aleksandr. "Theory and Practice of Prion Protein Analysis in Food Products." Foods and Raw Materials 2, no. 2 (September 1, 2014): 106–20. http://dx.doi.org/10.12737/5467.

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Fleming, Eleanor, Andy H. Yuan, Danielle M. Heller, and Ann Hochschild. "A bacteria-based genetic assay detects prion formation." Proceedings of the National Academy of Sciences 116, no. 10 (February 19, 2019): 4605–10. http://dx.doi.org/10.1073/pnas.1817711116.

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Prions are infectious, self-propagating protein aggregates that are notorious for causing devastating neurodegenerative diseases in mammals. Recent evidence supports the existence of prions in bacteria. However, the evaluation of candidate bacterial prion-forming proteins has been hampered by the lack of genetic assays for detecting their conversion to an aggregated prion conformation. Here we describe a bacteria-based genetic assay that distinguishes cells carrying a model yeast prion protein in its nonprion and prion forms. We then use this assay to investigate the prion-forming potential of single-stranded DNA-binding protein (SSB) ofCampylobacter hominis. Our findings indicate that SSB possesses a prion-forming domain that can transition between nonprion and prion conformations. Furthermore, we show that bacterial cells can propagate the prion form over 100 generations in a manner that depends on the disaggregase ClpB. The bacteria-based genetic tool we present may facilitate the investigation of prion-like phenomena in all domains of life.

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Sprunger, Macy L., and Meredith E. Jackrel. "Prion-Like Proteins in Phase Separation and Their Link to Disease." Biomolecules 11, no. 7 (July 11, 2021): 1014. http://dx.doi.org/10.3390/biom11071014.

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Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-like regions have also been found to drive liquid-liquid phase separation. Liquid-liquid phase separation is thought to be an important physiological process, but one that is prone to malfunction. Thus, aberrant liquid-to-solid phase transitions may drive protein aggregation and fibrillization, which could give rise to pathological inclusions. Here, we review prions and prion-like proteins, their roles in phase separation and disease, as well as potential therapeutic approaches to counter aberrant phase transitions.

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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 studied extensively, it is still unclear what exactly drives PrP molecules into an infectious, self-templating conformation. In this review, we discuss crucial steps in the life cycle of prions that have been revealed inex vivomodels. Importantly, the persistent propagation of prions in mitotically active cells argues that cellular processes are in place that not only allow recruitment of cellular PrP into growing prion aggregates but also enable the multiplication of infectious seeds that are transmitted to daughter cells. Comparison of prions with other protein aggregates demonstrates that not all the characteristics of prions are equally shared by prion-like aggregates. Future experiments may reveal to which extent aggregation-prone proteins associated with other neurodegenerative diseases can copy the replication strategies of prions.

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Wickner, Reed B., Herman K. Edskes, Moonil Son, Songsong Wu, and Madaleine Niznikiewicz. "How Do Yeast Cells Contend with Prions?" International Journal of Molecular Sciences 21, no. 13 (July 3, 2020): 4742. http://dx.doi.org/10.3390/ijms21134742.

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Infectious proteins (prions) include an array of human (mammalian) and yeast amyloid diseases in which a protein or peptide forms a linear β-sheet-rich filament, at least one functional amyloid prion, and two functional infectious proteins unrelated to amyloid. In Saccharomyces cerevisiae, at least eight anti-prion systems deal with pathogenic amyloid yeast prions by (1) blocking their generation (Ssb1,2, Ssz1, Zuo1), (2) curing most variants as they arise (Btn2, Cur1, Hsp104, Upf1,2,3, Siw14), and (3) limiting the pathogenicity of variants that do arise and propagate (Sis1, Lug1). Known mechanisms include facilitating proper folding of the prion protein (Ssb1,2, Ssz1, Zuo1), producing highly asymmetric segregation of prion filaments in mitosis (Btn2, Hsp104), competing with the amyloid filaments for prion protein monomers (Upf1,2,3), and regulation of levels of inositol polyphosphates (Siw14). It is hoped that the discovery of yeast anti-prion systems and elucidation of their mechanisms will facilitate finding analogous or homologous systems in humans, whose manipulation may be useful in treatment.

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44

Piening, Niklas, Petra Weber, Tobias Högen, Michael Beekes, Hans Kretzschmar, and Armin Giese. "Photo-induced crosslinking of prion protein oligomers and prions." Amyloid 13, no. 2 (January 2006): 67–77. http://dx.doi.org/10.1080/13506120600722498.

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45

Montrasio, F., A. Cozzio, E. Flechsig, D. Rossi, M. A. Klein, T. Rulicke, A. J. Raeber, et al. "B lymphocyte-restricted expression of prion protein does not enable prion replication in prion protein knockout mice." Proceedings of the National Academy of Sciences 98, no. 7 (March 13, 2001): 4034–37. http://dx.doi.org/10.1073/pnas.051609398.

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46

Poggiolini, Ilaria, Daniela Saverioni, and Piero Parchi. "Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions." International Journal of Cell Biology 2013 (2013): 1–24. http://dx.doi.org/10.1155/2013/910314.

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Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species. The central event in TSE pathogenesis is the conformational conversion of the cellular prion protein,PrPC, into the aggregate,β-sheet rich, amyloidogenic form,PrPSc. Increasing evidence indicates that distinctPrPScconformers, forming distinct ordered aggregates, can encipher the phenotypic TSE variants related to prion strains. Prion strains are TSE isolates that, after inoculation into syngenic hosts, cause disease with distinct characteristics, such as incubation period, pattern ofPrPScdistribution, and regional severity of histopathological changes in the brain. In analogy with other amyloid forming proteins,PrPSctoxicity is thought to derive from the existence of various intermediate structures prior to the amyloid fiber formation and/or their specific interaction with membranes. The latter appears particularly relevant for the pathogenesis of TSEs associated with GPI-anchoredPrPSc, which involves major cellular membrane distortions in neurons. In this review, we update the current knowledge on the molecular mechanisms underlying three fundamental aspects of the basic biology of prions such as the putative mechanism of prion protein conversion to the pathogenic formPrPScand its propagation, the molecular basis of prion strains, and the mechanism of induced neurotoxicity byPrPScaggregates.

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MacLea, Kyle S., Kacy R. Paul, Zobaida Ben-Musa, Aubrey Waechter, Jenifer E. Shattuck, Margaret Gruca, and Eric D. Ross. "Distinct Amino Acid Compositional Requirements for Formation and Maintenance of the [PSI+] Prion in Yeast." Molecular and Cellular Biology 35, no. 5 (December 29, 2014): 899–911. http://dx.doi.org/10.1128/mcb.01020-14.

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Multiple yeast prions have been identified that result from the structural conversion of proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires a series of discrete steps. First, the prion protein must form an amyloid nucleus that can recruit and structurally convert additional soluble proteins. Subsequently, maintenance of the prion during cell division requires fragmentation of these aggregates to create new heritable propagons. For theSaccharomyces cerevisiaeprion protein Sup35, these different activities are encoded by different regions of the Sup35 prion domain. An N-terminal glutamine/asparagine-rich nucleation domain is required for nucleation and fiber growth, while an adjacent oligopeptide repeat domain is largely dispensable for prion nucleation and fiber growth but is required for chaperone-dependent prion maintenance. Although prion activity of glutamine/asparagine-rich proteins is predominantly determined by amino acid composition, the nucleation and oligopeptide repeat domains of Sup35 have distinct compositional requirements. Here, we quantitatively define these compositional requirementsin vivo. We show that aromatic residues strongly promote both prion formation and chaperone-dependent prion maintenance. In contrast, nonaromatic hydrophobic residues strongly promote prion formation but inhibit prion propagation. These results provide insight into why some aggregation-prone proteins are unable to propagate as prions.

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48

Mironova, Ludmila N. "Protein inheritance and regulation of gene expression in yeast." Ecological genetics 8, no. 4 (December 15, 2010): 10–16. http://dx.doi.org/10.17816/ecogen8410-16.

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Prions of lower eukaryotes are genetic determinants of protein nature. Last years are marked by rapid development of the conception of prion inheritance. The list of yeast proteins, which have been shown to exist in the prion form in vivo, and phenotypic manifestation of prions provide good reason to believe that protein prionization may represent epigenetic mechanism regulating adaptability of a single cell and cellular population to environmental conditions.

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Nicoll, Andrew, and John Collinge. "Preventing Prion Pathogenicity by Targeting the Cellular Prion Protein." Infectious Disorders - Drug Targets 9, no. 1 (February 1, 2009): 48–57. http://dx.doi.org/10.2174/1871526510909010048.

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Rigter, Alan, Jan Priem, Jan P. M. Langeveld, and Alex Bossers. "Prion protein self-interaction in prion disease therapy approaches." Veterinary Quarterly 31, no. 3 (September 2011): 115–28. http://dx.doi.org/10.1080/01652176.2011.604976.

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Journal articles on the topic 'Prion protein'

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