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Journal articles on the topic 'Prion conversion'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

Jones, Rachel. "Blocking prion conversion." Nature Reviews Neuroscience 2, no. 9 (2001): 605. http://dx.doi.org/10.1038/35090100.

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2

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

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Hara, Hideyuki, and Suehiro Sakaguchi. "Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion." International Journal of Molecular Sciences 22, no. 22 (2021): 12439. http://dx.doi.org/10.3390/ijms222212439.

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Conformational conversion of the cellular isoform of prion protein, PrPC, into the abnormally folded, amyloidogenic isoform, PrPSc, is an underlying pathogenic mechanism in prion diseases. The diseases manifest as sporadic, hereditary, and acquired disorders. Etiological mechanisms driving the conversion of PrPC into PrPSc are unknown in sporadic prion diseases, while prion infection and specific mutations in the PrP gene are known to cause the conversion of PrPC into PrPSc in acquired and hereditary prion diseases, respectively. We recently reported that a neurotropic strain of influenza A vi

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Rigter, Alan, Jan Priem, Drophatie Timmers-Parohi, Jan PM Langeveld, Fred G. van Zijderveld, and Alex Bossers. "Prion protein self-peptides modulate prion interactions and conversion." BMC Biochemistry 10, no. 1 (2009): 29. http://dx.doi.org/10.1186/1471-2091-10-29.

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5

Shen, Liang, and Hong-Fang Ji. "Conformational conversion and prion disease." Nature Reviews Molecular Cell Biology 12, no. 4 (2011): 273. http://dx.doi.org/10.1038/nrm3007-c1.

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6

Supattapone, Surachai. "Prion protein conversion in vitro." Journal of Molecular Medicine 82, no. 6 (2004): 348–56. http://dx.doi.org/10.1007/s00109-004-0534-3.

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Davenport, Kristen A., Davin M. Henderson, Candace K. Mathiason, and Edward A. Hoover. "Assessment of the PrP c Amino-Terminal Domain in Prion Species Barriers." Journal of Virology 90, no. 23 (2016): 10752–61. http://dx.doi.org/10.1128/jvi.01121-16.

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ABSTRACT Chronic wasting disease (CWD) in cervids and bovine spongiform encephalopathy (BSE) in cattle are prion diseases that are caused by the same protein-misfolding mechanism, but they appear to pose different risks to humans. We are interested in understanding the differences between the species barriers of CWD and BSE. We used real-time, quaking-induced conversion (RT-QuIC) to model the central molecular event in prion disease, the templated misfolding of the normal prion protein, PrP c , to a pathogenic, amyloid isoform, scrapie prion protein, PrP Sc . We examined the role of the PrP c

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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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Engelke, Anna D., Anika Gonsberg, Simrika Thapa, et al. "Dimerization of the cellular prion protein inhibits propagation of scrapie prions." Journal of Biological Chemistry 293, no. 21 (2018): 8020–31. http://dx.doi.org/10.1074/jbc.ra117.000990.

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A central step in the pathogenesis of prion diseases is the conformational transition of the cellular prion protein (PrPC) into the scrapie isoform, denoted PrPSc. Studies in transgenic mice have indicated that this conversion requires a direct interaction between PrPC and PrPSc; however, insights into the underlying mechanisms are still missing. Interestingly, only a subfraction of PrPC is converted in scrapie-infected cells, suggesting that not all PrPC species are suitable substrates for the conversion. On the basis of the observation that PrPC can form homodimers under physiological condit

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10

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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11

Davenport, Kristen A., Davin M. Henderson, Jifeng Bian, Glenn C. Telling, Candace K. Mathiason, and Edward A. Hoover. "Insights into Chronic Wasting Disease and Bovine Spongiform Encephalopathy Species Barriers by Use of Real-Time Conversion." Journal of Virology 89, no. 18 (2015): 9524–31. http://dx.doi.org/10.1128/jvi.01439-15.

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ABSTRACTThe propensity for transspecies prion transmission is related to the structural characteristics of the enciphering and new host PrP, although the exact mechanism remains incompletely understood. The effects of variability in prion protein on cross-species prion transmission have been studied with animal bioassays, but the influence of prion protein structure versus that of host cofactors (e.g., cellular constituents, trafficking, and innate immune interactions) remains difficult to dissect. To isolate the effects of protein-protein interactions on transspecies conversion, we used recom

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12

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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13

Deleault, Nathan R., Ralf W. Lucassen, and Surachai Supattapone. "RNA molecules stimulate prion protein conversion." Nature 425, no. 6959 (2003): 717–20. http://dx.doi.org/10.1038/nature01979.

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14

Apostol, Marcin I., and Witold K. Surewicz. "Structural Underpinnings of Prion Protein Conversion." Journal of Biological Chemistry 286, no. 21 (2011): le7. http://dx.doi.org/10.1074/jbc.l110.213926.

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15

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

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Fernández, María Rosario, Cristina Batlle, Marcos Gil-García, and Salvador Ventura. "Amyloid cores in prion domains: Key regulators for prion conformational conversion." Prion 11, no. 1 (2017): 31–39. http://dx.doi.org/10.1080/19336896.2017.1282020.

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17

Legname, Giuseppe. "Copper coordination modulates prion conversion and infectivity in mammalian prion proteins." Prion 17, no. 1 (2023): 1–6. http://dx.doi.org/10.1080/19336896.2022.2163835.

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18

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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Thapa, Simrika, Basant Abdulrahman, Dalia H. Abdelaziz, Li Lu, Manel Ben Aissa, and Hermann M. Schatzl. "Overexpression of quality control proteins reduces prion conversion in prion-infected cells." Journal of Biological Chemistry 293, no. 41 (2018): 16069–82. http://dx.doi.org/10.1074/jbc.ra118.002754.

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Prion diseases are fatal infectious neurodegenerative disorders in humans and other animals and are caused by misfolding of the cellular prion protein (PrPC) into the pathological isoform PrPSc. These diseases have the potential to transmit within or between species, including zoonotic transmission to humans. Elucidating the molecular and cellular mechanisms underlying prion propagation and transmission is therefore critical for developing molecular strategies for disease intervention. We have shown previously that impaired quality control mechanisms directly influence prion propagation. In th

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Hara, Hideyuki, and Suehiro Sakaguchi. "N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases." International Journal of Molecular Sciences 21, no. 17 (2020): 6233. http://dx.doi.org/10.3390/ijms21176233.

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The normal cellular isoform of prion protein, designated PrPC, is constitutively converted to the abnormally folded, amyloidogenic isoform, PrPSc, in prion diseases, which include Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy in animals. PrPC is a membrane glycoprotein consisting of the non-structural N-terminal domain and the globular C-terminal domain. During conversion of PrPC to PrPSc, its 2/3 C-terminal region undergoes marked structural changes, forming a protease-resistant structure. In contrast, the N-terminal region remains protease-sensitive in

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21

Rigter, Alan, and Alex Bossers. "Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion." Journal of General Virology 86, no. 9 (2005): 2627–34. http://dx.doi.org/10.1099/vir.0.80901-0.

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Conversion of the host-encoded protease-sensitive cellular prion protein (PrPC) into the scrapie-associated protease-resistant isoform (PrPSc) of prion protein (PrP) is the central event in transmissible spongiform encephalopathies or prion diseases. Differences in transmissibility and susceptibility are largely determined by polymorphisms in PrP, but the exact molecular mechanism behind PrP conversion and the modulation by disease-associated polymorphisms is still unclear. To assess whether the polymorphisms in either PrPC or PrPSc modulate the initial binding of PrPC to PrPSc, several natura

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22

Baral, Pravas, Mridula Swayampakula, Manoj Rout, Leo Spyracopoulos, Adriano Aguzzi, and Michael James. "Structural Basis of Prion Protein Conformation Conversion Inhibition." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C812. http://dx.doi.org/10.1107/s2053273314091876.

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Prion diseases are fatal neurodegenerative diseases that affect humans and other animals. A conformational transition of the cellular prion protein, PrPC, into an infectious isoform, PrPSc, is the central event leading to aggregation and the fatal progression of these diseases. One of the therapeutic approaches for the prion diseases is the use of pharmacological chaperones. These molecules can stabilize the prion protein in its native conformation and can arrest the disease progression. Tricyclic phenothiazine compounds exhibit anti-prion activity; however, the underlying molecular mechanism

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23

Ma, Jiyan, Jingjing Zhang, and Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers." Viruses 14, no. 9 (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 recapitulat

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24

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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25

Kazlauskaite, Jurate, and Teresa JT Pinheiro. "Binding of prion proteins to lipid membranes and implications for prion conversion." Biochemical Society Transactions 30, no. 3 (2002): A95. http://dx.doi.org/10.1042/bst030a095b.

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26

Sanghera, Narinder, and Teresa J. T. Pinheiro. "Binding of prion protein to lipid membranes and implications for prion conversion." Journal of Molecular Biology 315, no. 5 (2002): 1241–56. http://dx.doi.org/10.1006/jmbi.2001.5322.

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27

Caughey, Byron. "Prion protein interconversions†." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 356, no. 1406 (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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Saleem, Fozia, Trent C. Bjorndahl, Carol L. Ladner, Rolando Perez-Pineiro, Burim N. Ametaj, and David S. Wishart. "Lipopolysaccharide induced conversion of recombinant prion protein." Prion 8, no. 2 (2014): 221–32. http://dx.doi.org/10.4161/pri.28939.

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Gill, Andrew C., Sonya Agarwal, Teresa J. T. Pinheiro, and James F. Graham. "Structural requirements for efficient prion protein conversion." Prion 4, no. 4 (2010): 235–43. http://dx.doi.org/10.4161/pri.4.4.13394.

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30

Carter, John, Audrius Zukas, Cathrin Bruederle, Audrius A. Zukas, Cathrin E. Bruederle, and John Mark Carter. "Sonication Induced Intermediate in Prion Protein Conversion." Protein & Peptide Letters 15, no. 2 (2008): 206–11. http://dx.doi.org/10.2174/092986608783489517.

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31

Tuite, Mick F., and Tricia R. Serio. "Conformational conversion and prion disease: authors' reply." Nature Reviews Molecular Cell Biology 12, no. 4 (2011): 273. http://dx.doi.org/10.1038/nrm3007-c2.

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32

Wang, Fei, Xinhe Wang, and Jiyan Ma. "Conversion of bacterially expressed recombinant prion protein." Methods 53, no. 3 (2011): 208–13. http://dx.doi.org/10.1016/j.ymeth.2010.12.013.

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33

Atarashi, Ryuichiro, Valerie L. Sim, Noriyuki Nishida, Byron Caughey, and Shigeru Katamine. "Prion Strain-Dependent Differences in Conversion of Mutant Prion Proteins in Cell Culture." Journal of Virology 80, no. 16 (2006): 7854–62. http://dx.doi.org/10.1128/jvi.00424-06.

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ABSTRACT Although the protein-only hypothesis proposes that it is the conformation of abnormal prion protein (PrPSc) that determines strain diversity, the molecular basis of strains remains to be elucidated. In the present study, we generated a series of mutations in the normal prion protein (PrPC) in which a single glutamine residue was replaced with a basic amino acid and compared their abilities to convert to PrPSc in cultured neuronal N2a58 cells infected with either the Chandler or 22L mouse-adapted scrapie strain. In mice, these strains generate PrPSc of the same sequence but different c

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Barria, Marcelo A., Adriana Libori, Gordon Mitchell, and Mark W. Head. "Susceptibility of Human Prion Protein to Conversion by Chronic Wasting Disease Prions." Emerging Infectious Diseases 24, no. 8 (2018): 1482–89. http://dx.doi.org/10.3201/eid2408.161888.

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35

McMahon, Hilary E. M. "Prion processing: a double-edged sword?" Biochemical Society Transactions 40, no. 4 (2012): 735–38. http://dx.doi.org/10.1042/bst20120031.

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The events leading to the degradation of the endogenous PrPC (normal cellular prion protein) have been the subject of numerous studies. Two cleavage processes, α-cleavage and β-cleavage, are responsible for the main C- and N-terminal fragments produced from PrPC. Both cleavage processes occur within the N-terminus of PrPC, a region that is significant in terms of function. α-Cleavage, an enzymatic event that occurs at amino acid residues 110 and 111 on PrPC, interferes with the conversion of PrPC into the prion disease-associated isoform, PrPSc (abnormal disease-specific conformation of prion

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Orge, Leonor, Carla Lima, Carla Machado, et al. "Neuropathology of Animal Prion Diseases." Biomolecules 11, no. 3 (2021): 466. http://dx.doi.org/10.3390/biom11030466.

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Transmissible Spongiform Encephalopathies (TSEs) or prion diseases are a fatal group of infectious, inherited and spontaneous neurodegenerative diseases affecting human and animals. They are caused by the conversion of cellular prion protein (PrPC) into a misfolded pathological isoform (PrPSc or prion- proteinaceous infectious particle) that self-propagates by conformational conversion of PrPC. Yet by an unknown mechanism, PrPC can fold into different PrPSc conformers that may result in different prion strains that display specific disease phenotype (incubation time, clinical signs and lesion

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Kang, Hae-Eun, Jifeng Bian, Sarah J. Kane, et al. "Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination." Journal of Biological Chemistry 295, no. 30 (2020): 10420–33. http://dx.doi.org/10.1074/jbc.ra120.012796.

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The causative factors underlying conformational conversion of cellular prion protein (PrPC) into its infectious counterpart (PrPSc) during prion infection remain undetermined, in part because of a lack of monoclonal antibodies (mAbs) that can distinguish these conformational isoforms. Here we show that the anti-PrP mAb PRC7 recognizes an epitope that is shielded from detection when glycans are attached to Asn-196. We observed that whereas PrPC is predisposed to full glycosylation and is therefore refractory to PRC7 detection, prion infection leads to diminished PrPSc glycosylation at Asn-196,

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Choi, Jin-Kyu, Ignazio Cali, Krystyna Surewicz, Qingzhong Kong, Pierluigi Gambetti, and Witold K. Surewicz. "Amyloid fibrils from the N-terminal prion protein fragment are infectious." Proceedings of the National Academy of Sciences 113, no. 48 (2016): 13851–56. http://dx.doi.org/10.1073/pnas.1610716113.

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Recombinant C-terminally truncated prion protein PrP23-144 (which corresponds to the Y145Stop PrP variant associated with a Gerstmann–Sträussler–Scheinker-like prion disease) spontaneously forms amyloid fibrils with a parallel in-register β-sheet architecture and β-sheet core mapping to residues ∼112–139. Here we report that mice (bothtga20and wild type) inoculated with a murine (moPrP23-144) version of these fibrils develop clinical prion disease with a 100% attack rate. Remarkably, even though fibrils in the inoculum lack the entire C-terminal domain of PrP, brains of clinically sick mice ac

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Tamgüney, Gültekin, Kurt Giles, David V. Glidden, et al. "Genes contributing to prion pathogenesis." Journal of General Virology 89, no. 7 (2008): 1777–88. http://dx.doi.org/10.1099/vir.0.2008/001255-0.

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Prion diseases are caused by conversion of a normally folded, non-pathogenic isoform of the prion protein (PrPC) to a misfolded, pathogenic isoform (PrPSc). Prion inoculation experiments in mice expressing homologous PrPC molecules on different genetic backgrounds displayed different incubation times, indicating that the conversion reaction may be influenced by other gene products. To identify genes that contribute to prion pathogenesis, we analysed incubation times of prions in mice in which the gene product was inactivated, knocked out or overexpressed. We tested 20 candidate genes, because

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Atarashi, Ryuichiro, Roger A. Moore, Valerie L. Sim, et al. "Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein." Nature Methods 4, no. 8 (2007): 645–50. http://dx.doi.org/10.1038/nmeth1066.

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do Carmo Ferreira, Natália, and Byron Caughey. "Cell-free prion protein conversion assays in screening for anti-prion drug candidates." Current Opinion in Pharmacology 44 (February 2019): 1–7. http://dx.doi.org/10.1016/j.coph.2018.10.001.

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Caughey, B., and G. S. Baron. "Factors affecting interactions between prion protein isoforms." Biochemical Society Transactions 30, no. 4 (2002): 565–69. http://dx.doi.org/10.1042/bst0300565.

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Interactions between normal, protease-sensitive prion protein (PrP-sen or PrPc) and its protease-resistant isoform (PrP-res or PrPsc) are critical in transmissible spongiform encephalopathy (TSE) diseases. To investigate the propagation of PrP-res between cells we tested whether PrP-res in scrapie brain microsomes can induce the conversion of PrP-sen to PrP-res if the PrP-sen is bound to uninfected raft membranes. Surprisingly, no conversion was observed unless the microsomal and raft membranes were fused or PrP-sen was released from raft membranes. These results suggest that the propagation o

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Delmouly, Karine, Maxime Belondrade, Danielle Casanova, Ollivier Milhavet, and Sylvain Lehmann. "HEPES inhibits the conversion of prion protein in cell culture." Journal of General Virology 92, no. 5 (2011): 1244–50. http://dx.doi.org/10.1099/vir.0.027334-0.

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HEPES is a well-known buffering reagent used in cell-culture medium. Interestingly, this compound is also responsible for significant modifications of biological parameters such as uptake of organic molecules, alteration of oxidative stress mechanisms or inhibition of ion channels. While using cell-culture medium supplemented with HEPES on prion-infected cells, it was noticed that there was a significant concentration-dependent inhibition of accumulation of the abnormal isoform of the prion protein (PrPSc). This effect was present only in live cells and was thought to be related to modificatio

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Singh, Serena, and Mari L. DeMarco. "In Vitro Conversion Assays Diagnostic for Neurodegenerative Proteinopathies." Journal of Applied Laboratory Medicine 5, no. 1 (2019): 142–57. http://dx.doi.org/10.1373/jalm.2019.029801.

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Abstract Background In vitro conversion assays, including real-time quaking-induced conversion (RT-QuIC) and protein misfolding cyclic amplification (PMCA) techniques, were first developed to study the conversion process of the prion protein to its misfolded, disease-associated conformation. The intrinsic property of prion proteins to propagate their misfolded structure was later exploited to detect subfemtogram quantities of the misfolded protein present in tissues and fluids from humans and animals with transmissible spongiform encephalopathies. Currently, conversion assays are used clinical

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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 (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

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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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Kazlauskaite, Jurate, and Teresa J. T. Pinheiro. "Aggregation and fibrillization of prions in lipid membranes." Biochemical Society Symposia 72 (January 1, 2005): 211–22. http://dx.doi.org/10.1042/bss0720211.

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Abstract:

A key molecular event in prion diseases is the conversion of PrP (prion protein) from its normal cellular form (PrPc) into the disease-specific form (PrPSc). The transition from PrPc to PrPSc involves a major conformational change, resulting in amorphous aggregates and/or fibrillar amyloid deposits. Here, we review several lines of evidence implicating membranes in the conversion of PrP, and summarize recent results from our own work on the role of lipid membranes in conformational transitions of prion proteins. By establishing new correlations between in vivo biological findings with in vitro

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DOWNING, Donald T., та N. D. LAZO. "Molecular modelling indicates that the pathological conformations of prion proteins might be β-helical". Biochemical Journal 343, № 2 (1999): 453–60. http://dx.doi.org/10.1042/bj3430453.

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Creutzfeldt-Jakob disease, kuru, scrapie and bovine spongiform encephalopathy are diseases of the mammalian central nervous system that involve the conversion of a cellular protein into an insoluble extracellular isoform. Spectroscopic studies have shown that the precursor protein contains mainly α-helical and random-coil conformations, whereas the prion isoform is largely in the β conformation. The pathogenic prion is resistant to denaturation and protease digestion and can promote the conversion of the precursor protein to the pathogenic form. These properties have yet to be explained in ter

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Legname, Giuseppe. "Early structural features in mammalian prion conformation conversion." Prion 6, no. 1 (2012): 37–39. http://dx.doi.org/10.4161/pri.6.1.18425.

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Spagnolli, Giovanni, Marta Rigoli, Simone Orioli, et al. "Full atomistic model of prion structure and conversion." PLOS Pathogens 15, no. 7 (2019): e1007864. http://dx.doi.org/10.1371/journal.ppat.1007864.

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