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Journal articles on the topic 'Prion protein gene'

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Published: 4 June 2021

Last updated: 30 January 2023

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1

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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2

Nakamura, Yuko, Akikazu Sakudo, Keiichi Saeki, Tomomi Kaneko, Yoshitsugu Matsumoto, Antonio Toniolo, Shigeyoshi Itohara, and Takashi Onodera. "Transfection of prion protein gene suppresses coxsackievirus B3 replication in prion protein gene-deficient cells." Journal of General Virology 84, no. 12 (December 1, 2003): 3495–502. http://dx.doi.org/10.1099/vir.0.19222-0.

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The susceptibility of prion protein gene (Prnp)-null cells to coxsackievirus B3 (CVB3) was investigated. Primary cultures of murine Prnp −/− brain cells were more sensitive to CVBs than corresponding cells from wild-type mice. The viral susceptibility of a Prnp-null cell line (HpL3-4) derived from the murine hippocampus was compared with that of two established cell lines (HeLa and HEp-2) that are widely employed for CVB3 studies. After infection with CVB3, HpL3-4 cells showed a very rapid and complete cytopathic effect (CPE). CPE developed earlier and viruses replicated at higher titres in HpL3-4 cells compared with HeLa and HEp-2 cells. Under a semi-solid medium, plaques developed rapidly in CVB3-infected HpL3-4 cells. To confirm the effect of Prnp on virus infection, a Prnp −/− cell line and a Prnp-transfected neuronal cell line were analysed. The replication and release of infectious particles of CVB3 in Prnp −/− cells were significantly more effective than those of the Prnp-transfected cell line. Levels of type I interferon (IFN) after CVB3 infection were higher in the Prnp-transfected cell line than in Prnp −/− cells, whereas apoptotic cells were more obvious in the Prnp −/− cells than in those of the Prnp-transfected cell line. These findings suggest that the absence of Prnp retards the induction of CVB3-induced IFNs, resulting in an enhanced CVB3 production and apoptotic cell death. Furthermore, our data indicate that the HpL3-4 cell line may provide a novel and sensitive system for isolation of CVB3 from clinical specimens.

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3

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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4

Caramelli, Paulo. "Prion protein gene in Alzheimer's disease." Arquivos de Neuro-Psiquiatria 71, no. 7 (July 2013): 419–20. http://dx.doi.org/10.1590/0004-282x20130093.

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5

Kovács, Gábor G., Gianriccardo Trabattoni, Johannes A. Hainfellner, James W. Ironside, Richard S. G. Knight, and Herbert Budka. "Mutations of the Prion Protein Gene." Journal of Neurology 249, no. 11 (November 1, 2002): 1567–82. http://dx.doi.org/10.1007/s00415-002-0896-9.

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6

Schätzl, Hermann M., Maria Da Costa, Leslie Taylor, Fred E. Cohen, and Stanley B. Prusiner. "Prion Protein Gene Variation Among Primates." Journal of Molecular Biology 245, no. 4 (January 1995): 362–74. http://dx.doi.org/10.1006/jmbi.1994.0030.

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7

Schätzl, Hermann M., Maria Da Costa, Leslie Taylor, Fred E. Cohen, and Stanley B. Prusiner. "Prion protein gene variation among primates." Journal of Molecular Biology 265, no. 2 (January 1997): 257. http://dx.doi.org/10.1006/jmbi.1996.0791.

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8

Mastrangelo, Peter, and David Westaway. "Biology of the prion gene complex." Biochemistry and Cell Biology 79, no. 5 (October 1, 2001): 613–28. http://dx.doi.org/10.1139/o01-142.

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The prion protein gene Prnp encodes PrPSc, the major structural component of prions, infectious pathogens causing a number of disorders including scrapie and bovine spongiform encephalopathy (BSE). Missense mutations in the human Prnp gene, PRNP, cause inherited prion diseases such as familial CreutzfeldtJakob Disease. In uninfected animals, Prnp encodes a GPI-anchored protein denoted PrPC, and in prion infections, PrPCis converted to PrPScby templated refolding. Although Prnp is conserved in mammalian species, attempts to verify interactions of putative PrP-binding proteins by genetic means have proven frustrating in that two independent lines of Prnp gene ablated mice (Prnp0/0mice: ZrchI and Npu) lacking PrPCremain healthy throughout development. This indicates that PrPCserves a function that is not apparent in a laboratory setting or that other molecules have overlapping functions. Shuttling or sequestration of synaptic Cu(II) via binding to N-terminal octapeptide residues and (or) signal transduction involving the fyn kinase are possibilities currently under consideration. A new point of entry into the issue of prion protein function has emerged from identification of a paralog, Prnd, with 25% coding sequence identity to Prnp. Prnd lies downstream of Prnp and encodes the Dpl protein. Like PrPC, Dpl is presented on the cell surface via a GPI anchor and has three α-helices: however, it lacks the conformationally plastic and octapeptide repeat domains present in its well-known relative. Interestingly, Dpl is overexpressed in two other lines of Prnp0/0mice (Ngsk and Rcm0) via intergenic splicing events. These lines of Prnp0/0mice exhibit ataxia and apoptosis of cerebellar cells, indicating that ectopic synthesis of Dpl protein is toxic to CNS neurons: this inference has now been confirmed by the construction of transgenic mice expressing Dpl under the direct control of the PrP promoter. Remarkably, Dpl-programmed ataxia is rescued by wt Prnp transgenes. The interaction between the Prnp and Prnd genes in mouse cerebellar neurons may have a physical correlate in competition between Dpl and PrPCwithin a common biochemical pathway that, when misregulated, leads to apoptosis.Key words: spongiform encephalopathy, neurodegenerative disease, paralogs, scrapie, CJD.

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9

Cardinale, Alessio, and Silvia Biocca. "Gene-Based Antibody Strategies for Prion Diseases." International Journal of Cell Biology 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/710406.

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Prion diseases or transmissible spongiform encephalopathies (TSE) are a group of neurodegenerative and infectious disorders characterized by the conversion of a normal cellular protein PrPCinto a pathological abnormally folded form, termed PrPSc. There are neither available therapies nor diagnostic tools for an early identification of individuals affected by these diseases. New gene-based antibody strategies are emerging as valuable therapeutic tools. Among these, intrabodies are chimeric molecules composed by recombinant antibody fragments fused to intracellular trafficking sequences, aimed at inhibiting,in vivo, the function of specific therapeutic targets. The advantage of intrabodies is that they can be selected against a precise epitope of target proteins, including protein-protein interaction sites and cytotoxic conformers (i.e., oligomeric and fibrillar assemblies). Herein, we address and discussin vitroandin vivoapplications of intrabodies in prion diseases, focussing on their therapeutic potential.

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10

Resende, Catarina G., Tiago F. Outeiro, Laina Sands, Susan Lindquist, and Mick F. Tuite. "Prion protein gene polymorphisms in Saccharomyces cerevisiae." Molecular Microbiology 49, no. 4 (July 4, 2003): 1005–17. http://dx.doi.org/10.1046/j.1365-2958.2003.03608.x.

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11

Sakudo, Akikazu, Takashi Onodera, and Kazuyoshi Ikuta. "Prion Protein Gene-Deficient Cell Lines: Powerful Tools for Prion Biology." Microbiology and Immunology 51, no. 1 (January 2007): 1–13. http://dx.doi.org/10.1111/j.1348-0421.2007.tb03877.x.

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12

Niżnikowski, Roman, Grzegorz Czub, Marcin Świątek, Magdalena Ślęzak, and Krzysztof Głowacz. "POLYMORPHISM OF THE PRION PROTEIN GENE IN MEAT AND WOOL-MEAT SHEEP BREEDS IN POLAND." Acta Scientiarum Polonorum Zootechnica 15, no. 3 (August 15, 2016): 3–14. http://dx.doi.org/10.21005/asp.2016.15.3.01.

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13

Van den Broeke, A., M. Van Poucke, A. Van Zeveren, and L. J. Peelman. "Ribosomal protein SA and its pseudogenes in ruminants: an extremely conserved gene family." Czech Journal of Animal Science 58, No. 2 (February 12, 2013): 79–90. http://dx.doi.org/10.17221/6618-cjas.

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The ribosomal protein SA (RPSA), also known as 37-kDa laminin receptor precursor/67-kDa laminin receptor (LRP/LR), has been identified as a multifunctional protein, playing an important role in multiple pathologies like cancer and prion diseases. Since RPSA is involved in the binding and internalization of the prion protein, mutations in the ovine RPSA gene, influencing the RPSA-PrP<sup>C</sup>/PrP<sup>Sc </sup>binding, can potentially play a part in the resistance to prion diseases. Our goal was to further characterize the complex RPSA gene family and to detect structural mutations which can play a role in this disease. In a prior study, 11 ovine pseudogenes were detected experimentally. As the whole genome shotgun ovine genome became accessible, an in silico genome-wide screening was performed and 37 new pseudogenes (36 processed and one semi-processed pseudogene) were detected, bringing the total to 48 ovine RPSA pseudogenes. Additionally, the complete bovine genome was screened in silico and 56 pseudogenes were identified. Once these sequences were known, it was possible to analyze the presence of mutations in the coding sequence and exon-flanking regions of the ovine functional full-length RPSA gene without the interference of pseudogenic sequences. Nineteen mutations were found: one in the 5’ UTR, a silent one in the coding region, and seventeen in the exon-flanking regions, including an interesting mutation in the SNORA62 gene, localized in intron 4 of RPSA, leading to potential ribosomal defects. Structural mutations of the RPSA gene can be ruled out to play a role in transmissible spongiform encephalopathies but regulatory mutations still can have an effect on these diseases.

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14

Slate, Jon. "Molecular evolution of the sheep prion protein gene." Proceedings of the Royal Society B: Biological Sciences 272, no. 1579 (September 20, 2005): 2371–77. http://dx.doi.org/10.1098/rspb.2005.3259.

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15

Richt, Jürgen A., and S. Mark Hall. "BSE Case Associated with Prion Protein Gene Mutation." PLoS Pathogens 4, no. 9 (September 12, 2008): e1000156. http://dx.doi.org/10.1371/journal.ppat.1000156.

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16

Kretzschmar, H. A., M. Neumann, G. Riethmuller, and S. B. Prusiner. "Molecular cloning of a mink prion protein gene." Journal of General Virology 73, no. 10 (October 1, 1992): 2757–61. http://dx.doi.org/10.1099/0022-1317-73-10-2757.

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17

Abe, E., C. Wada, T. Hatakeyama, F. Takeda, K. Obara, M. Kobayashi, T. Imota, et al. "Clinical benefit of the prion protein gene screening." Journal of the Neurological Sciences 357 (October 2015): e109. http://dx.doi.org/10.1016/j.jns.2015.08.349.

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18

Billinis, Charalambos, Cynthia H. Panagiotidis, Vassilios Psychas, Stamatis Argyroudis, Anna Nicolaou, Sotirios Leontides, Orestis Papadopoulos, and Theodoros Sklaviadis. "Prion protein gene polymorphisms in natural goat scrapie." Journal of General Virology 83, no. 3 (March 1, 2002): 713–21. http://dx.doi.org/10.1099/0022-1317-83-3-713.

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A total of 51 goats, including seven clinical cases, from the first herd in Greece reported to have scrapie was examined to discern an association between scrapie susceptibility and polymorphisms of the gene encoding the prion protein (PrP). Each animal was evaluated for clinical signs of the disease, histopathological lesions associated with scrapie, the presence of detectable protease-resistant PrP in the brain and PrP genotype. Eleven different PrP genotypes encoding at least five unique predicted mature PrP amino acid sequences were found. These genotypes included the amino acid polymorphisms at codons 143 (H→R) and 240 (S→P) and ‘silent’ nucleotide alterations at codons 42 (a→g) and 138 (c→t). Additionally, novel caprine amino acid polymorphisms were detected at codons 21 (V→A), 23 (L→P), 49 (G→S), 154 (R→H), 168 (P→Q) and 220 (Q→H) and new silent mutations were found at codons 107 (g→a) and 207 (g→a). The following variants were found in scrapie-affected goats: VV21, LL23, GG49, SS49, HH143, HR143, RR154, PP168, PP240, SP240 and SS240. All scrapie-affected animals carried the HH143RR154 genotype, with the exception of two goats (HR143), both of which had detectable protease-resistant PrP but showed no clinical signs or histopathological lesions characteristic of scrapie.

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19

Palmer, Mark S., and John Collinge. "Mutations and polymorphisms in the prion protein gene." Human Mutation 2, no. 3 (1993): 168–73. http://dx.doi.org/10.1002/humu.1380020303.

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20

McKinley, Michael P., Bruce Hay, Vishwanath R. Lingappa, Ivan Lieberburg, and Stanley B. Prusiner. "Developmental expression of prion protein gene in brain." Developmental Biology 121, no. 1 (May 1987): 105–10. http://dx.doi.org/10.1016/0012-1606(87)90143-6.

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21

Singh, Neena, Gianluigi Zanusso, Shu G. Chen, Hisashi Fujioka, Sandra Richardson, Pierluigi Gambetti, and Robert B. Petersen. "Prion Protein Aggregation Reverted by Low Temperature in Transfected Cells Carrying a Prion Protein Gene Mutation." Journal of Biological Chemistry 272, no. 45 (November 7, 1997): 28461–70. http://dx.doi.org/10.1074/jbc.272.45.28461.

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22

Thapa, Simrika, Cristobal Marrero Winkens, Waqas Tahir, Maria I. Arifin, Sabine Gilch, and Hermann M. Schatzl. "Gene-Edited Cell Models to Study Chronic Wasting Disease." Viruses 14, no. 3 (March 15, 2022): 609. http://dx.doi.org/10.3390/v14030609.

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Prion diseases are fatal infectious neurodegenerative disorders affecting both humans and animals. They are caused by the misfolded isoform of the cellular prion protein (PrPC), PrPSc, and currently no options exist to prevent or cure prion diseases. Chronic wasting disease (CWD) in deer, elk and other cervids is considered the most contagious prion disease, with extensive shedding of infectivity into the environment. Cell culture models provide a versatile platform for convenient quantification of prions, for studying the molecular and cellular biology of prions, and for performing high-throughput screening of potential therapeutic compounds. Unfortunately, only a very limited number of cell lines are available that facilitate robust and persistent propagation of CWD prions. Gene-editing using programmable nucleases (e.g., CRISPR-Cas9 (CC9)) has proven to be a valuable tool for high precision site-specific gene modification, including gene deletion, insertion, and replacement. CC9-based gene editing was used recently for replacing the PrP gene in mouse and cell culture models, as efficient prion propagation usually requires matching sequence homology between infecting prions and prion protein in the recipient host. As expected, such gene-editing proved to be useful for developing CWD models. Several transgenic mouse models were available that propagate CWD prions effectively, however, mostly fail to reproduce CWD pathogenesis as found in the cervid host, including CWD prion shedding. This is different for the few currently available knock-in mouse models that seem to do so. In this review, we discuss the available in vitro and in vivo models of CWD, and the impact of gene-editing strategies.

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23

Mead, Simon, Sarah Lloyd, and John Collinge. "Genetic Factors in Mammalian Prion Diseases." Annual Review of Genetics 53, no. 1 (December 3, 2019): 117–47. http://dx.doi.org/10.1146/annurev-genet-120213-092352.

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Mammalian prion diseases are a group of neurodegenerative conditions caused by infection of the central nervous system with proteinaceous agents called prions, including sporadic, variant, and iatrogenic Creutzfeldt-Jakob disease; kuru; inherited prion disease; sheep scrapie; bovine spongiform encephalopathy; and chronic wasting disease. Prions are composed of misfolded and multimeric forms of the normal cellular prion protein (PrP). Prion diseases require host expression of the prion protein gene ( PRNP) and a range of other cellular functions to support their propagation and toxicity. Inherited forms of prion disease are caused by mutation of PRNP, whereas acquired and sporadically occurring mammalian prion diseases are controlled by powerful genetic risk and modifying factors. Whereas some PrP amino acid variants cause the disease, others confer protection, dramatically altered incubation times, or changes in the clinical phenotype. Multiple mechanisms, including interference with homotypic protein interactions and the selection of the permissible prion strains in a host, play a role. Several non- PRNP factors have now been uncovered that provide insights into pathways of disease susceptibility or neurotoxicity.

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24

Crowell, Jenna, Andrew Hughson, Byron Caughey, and Richard A. Bessen. "Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype." Journal of Virology 89, no. 20 (August 5, 2015): 10427–41. http://dx.doi.org/10.1128/jvi.01586-15.

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ABSTRACTPhenotypic diversity in prion diseases can be specified by prion strains in which biological traits are propagated through an epigenetic mechanism mediated by distinct PrPScconformations. We investigated the role of host-dependent factors on phenotypic diversity of chronic wasting disease (CWD) in different host species that express the same prion protein gene (Prnp). Two CWD strains that have distinct biological, biochemical, and pathological features were identified in transgenic mice that express the Syrian golden hamster (SGH)Prnp. The CKY strain of CWD had a shorter incubation period than the WST strain of CWD, but after transmission to SGH, the incubation period of CKY CWD was ∼150 days longer than WST CWD. Limited proteinase K digestion revealed strain-specific PrPScpolypeptide patterns that were maintained in both hosts, but the solubility and conformational stability of PrPScdiffered for the CWD strains in a host-dependent manner. WST CWD produced PrPScamyloid plaques in the brain of the SGH that were partially insoluble and stable at a high concentration of protein denaturant. However, in transgenic mice, PrPScfrom WST CWD did not assemble into plaques, was highly soluble, and had low conformational stability. Similar studies using the HY and DY strains of transmissible mink encephalopathy resulted in minor differences in prion biological and PrPScproperties between transgenic mice and SGH. These findings indicate that host-specific pathways that are independent ofPrnpcan alter the PrPScconformation of certain prion strains, leading to changes in the biophysical properties of PrPSc, neuropathology, and clinical prion disease.IMPORTANCEPrions are misfolded pathogenic proteins that cause neurodegeneration in humans and animals. Transmissible prion diseases exhibit a spectrum of disease phenotypes and the basis of this diversity is encoded in the structure of the pathogenic prion protein and propagated by an epigenetic mechanism. In the present study, we investigated prion diversity in two hosts species that express the same prion protein gene. While prior reports have demonstrated that prion strain properties are stable upon infection of the same host species and prion protein genotype, our findings indicate that certain prion strains can undergo dramatic changes in biological properties that are not dependent on the prion protein. Therefore, host factors independent of the prion protein can affect prion diversity. Understanding how host pathways can modify prion disease phenotypes may provide clues on how to alter prion formation and lead to treatments for prion, and other, human neurodegenerative diseases of protein misfolding.

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25

Yousaf, Saba, Muhammad Ahmad, Siwen Wu, Muhammad Anjum Zia, Ishtiaq Ahmed, Hafiz M. N. Iqbal, Qingyou Liu, and Saif ur Rehman. "Cellular Prion Protein Role in Cancer Biology: Is It A Potential Therapeutic Target?" Biomedicines 10, no. 11 (November 7, 2022): 2833. http://dx.doi.org/10.3390/biomedicines10112833.

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Cancers are worldwide health concerns, whether they are sporadic or hereditary. The fundamental mechanism that causes somatic or oncogenic mutations and ultimately aids cancer development is still unknown. However, mammalian cells with protein-only somatic inheritance may also contribute to cancerous malignancies. Emerging data from a recent study show that prion-like proteins and prions (PrPC) are crucial entities that have a functional role in developing neurological disorders and cancer. Furthermore, excessive PrPC expression profiling has also been detected in non-neuronal tissues, such as the lymphoid cells, kidney, GIT, lung, muscle, and mammary glands. PrPC expression is strongly linked with the proliferation and metastasis of pancreatic, prostate, colorectal, and breast malignancies. Similarly, experimental investigation presented that the PrPC expression, including the prion protein-coding gene (PRNP) and p53 ag are directly associated with tumorigenicity and metastasis (tumor suppressor gene). The ERK2 (extracellular signal-regulated kinase) pathway also confers a robust metastatic capability for PrPC-induced epithelial to mesenchymal transition. Additionally, prions could alter the epigenetic regulation of genes and overactive the mitogen-activated protein kinase (MAPK) signaling pathway, which promotes the development of cancer in humans. Protein overexpression or suppression caused by a prion and prion-like proteins has also been linked to oncogenesis and metastasis. Meanwhile, additional studies have discovered resistance to therapeutic targets, highlighting the significance of protein expression levels as potential diagnostic indicators and therapeutic targets.

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26

Jeong, Min-Ju, and Byung-Hoon Jeong. "No polymorphisms in the coding region of the prion-like protein gene in Thoroughbred racehorses." Acta Veterinaria Hungarica 67, no. 2 (June 2019): 174–82. http://dx.doi.org/10.1556/004.2019.019.

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Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of an abnormal prion protein isoform (PrPSc), which is converted from the normal prion protein (PrPC). Prion diseases have been reported in an extensive number of species but not in horses up to now; therefore, horses are known to be a species resistant to prion diseases. The prion-like protein gene (PRND) is closely located downstream of the prion protein gene (PRNP) and the prion-like protein (Doppel) is a homologue with PrP. Previous studies have shown that an association between prion diseases and polymorphisms of the PRND gene is reported in the main hosts of prion diseases. Hence, we examined the genetic variations of the PRND gene in Thoroughbred horses. Interestingly, polymorphisms of the PRND gene were not detected. In addition, we conducted a comparative analysis of the amino acid sequences of the PRND gene to identify the differences between horses and other species. The amino acid sequence of the horse PRND gene showed the highest identity to that of sheep (83.7%), followed by that of goats, cattle and humans. To the best of our knowledge, this is the first genetic study of the PRND gene in horses.

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27

Kim, Yong-Chan, Sae-Young Won, and Byung-Hoon Jeong. "Identification of Prion Disease-Related Somatic Mutations in the Prion Protein Gene (PRNP) in Cancer Patients." Cells 9, no. 6 (June 17, 2020): 1480. http://dx.doi.org/10.3390/cells9061480.

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Prion diseases are caused by misfolded prion protein (PrPSc) and are accompanied by spongiform vacuolation of brain lesions. Approximately three centuries have passed since prion diseases were first discovered around the world; however, the exact role of certain factors affecting the causative agent of prion diseases is still debatable. In recent studies, somatic mutations were assumed to be cause of several diseases. Thus, we postulated that genetically unstable cancer tissue may cause somatic mutations in the prion protein gene (PRNP), which could trigger the onset of prion diseases. To identify somatic mutations in the PRNP gene in cancer tissues, we analyzed somatic mutations in the PRNP gene in cancer patients using the Cancer Genome Atlas (TCGA) database. In addition, to evaluate whether the somatic mutations in the PRNP gene in cancer patients had a damaging effect, we performed in silico analysis using PolyPhen-2, PANTHER, PROVEAN, and AMYCO. We identified a total of 48 somatic mutations in the PRNP gene, including 8 somatic mutations that are known pathogenic mutations of prion diseases. We identified significantly different distributions among the types of cancer, the mutation counts, and the ages of diagnosis between the total cancer patient population and cancer patients carrying somatic mutations in the PRNP gene. Strikingly, although invasive breast carcinoma and glioblastoma accounted for a high percentage of the total cancer patient population (9.9% and 5.4%, respectively), somatic mutations in the PRNP gene have not been identified in these two cancer types. We suggested the possibility that somatic mutations of the PRNP gene in glioblastoma can be masked by a diagnosis of prion disease. In addition, we found four aggregation-prone somatic mutations, these being L125F, E146Q, R151C, and K204N. To the best of our knowledge, this is the first specific analysis of the somatic mutations in the PRNP gene in cancer patients.

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28

Ryskalin, Larisa, Carla L. Busceti, Francesca Biagioni, Fiona Limanaqi, Pietro Familiari, Alessandro Frati, and Francesco Fornai. "Prion Protein in Glioblastoma Multiforme." International Journal of Molecular Sciences 20, no. 20 (October 15, 2019): 5107. http://dx.doi.org/10.3390/ijms20205107.

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The cellular prion protein (PrPc) is an evolutionarily conserved cell surface protein encoded by the PRNP gene. PrPc is ubiquitously expressed within nearly all mammalian cells, though most abundantly within the CNS. Besides being implicated in the pathogenesis and transmission of prion diseases, recent studies have demonstrated that PrPc contributes to tumorigenesis by regulating tumor growth, differentiation, and resistance to conventional therapies. In particular, PrPc over-expression has been related to the acquisition of a malignant phenotype of cancer stem cells (CSCs) in a variety of solid tumors, encompassing pancreatic ductal adenocarcinoma (PDAC), osteosarcoma, breast cancer, gastric cancer, and primary brain tumors, mostly glioblastoma multiforme (GBM). Thus, PrPc is emerging as a key in maintaining glioblastoma cancer stem cells’ (GSCs) phenotype, thereby strongly affecting GBM infiltration and relapse. In fact, PrPc contributes to GSCs niche’s maintenance by modulating GSCs’ stem cell-like properties while restraining them from differentiation. This is the first review that discusses the role of PrPc in GBM. The manuscript focuses on how PrPc may act on GSCs to modify their expression and translational profile while making the micro-environment surrounding the GSCs niche more favorable to GBM growth and infiltration.

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29

Manson, J., J. D. West, V. Thomson, P. McBride, M. H. Kaufman, and J. Hope. "The prion protein gene: a role in mouse embryogenesis?" Development 115, no. 1 (May 1, 1992): 117–22. http://dx.doi.org/10.1242/dev.115.1.117.

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The neural membrane glycoprotein PrP (prion protein) has a key role in the development of scrapie and related neurodegenerative diseases. During pathogenesis, PrP accumulates in and around cells of the brain from which it can be isolated in a disease-specific, protease-resistant form. Although the involvement of PrP in the pathology of these diseases has long been known, the normal function of PrP remains unknown. Previous studies have shown that the PrP gene is expressed tissue specifically in adult animals, the highest levels in the brain, with intermediate levels in heart and lung and low levels in spleen. Prenatally, PrP mRNA has been detected in the brain of rat and hamster just prior to birth. In this study we have examined the expression of the PrP gene during mouse embryonic development by in situ hybridisation and observed dramatic regional and temporal gene expression in the embryo. Transcripts were detected in developing brain and spinal cord by 13.5 days. In addition, PrP gene expression was detected in the peripheral nervous system, in ganglia and nerve trunks of the sympathetic nervous system and neural cell populations of sensory organs. Expression of the PrP gene was not limited to neuronal cells, but was also detected in specific non-neuronal cell populations of the 13.5 and 16.5 day embryos and in extra-embryonic tissues from 6.5 days. This cell-specific expression suggests a pleiotropic role for PrP during development.

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30

Varela-Nallar, L., L. Cuitino, J. P. Sagal, and N. C. Inestrosa. "Regulation of prion protein gene expression by heavy metals." Journal of Neurochemistry 81 (June 28, 2008): 5–6. http://dx.doi.org/10.1046/j.1471-4159.81.s1.1_4.x.

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31

Petersen, R. B., M. T. MD, L. B. MD, B. S. MD, R. M. Torack, S. L. MS, J. J. MD, et al. "Analysis of the prion protein gene in thalamic dementia." Neurology 42, no. 10 (October 1, 1992): 1859. http://dx.doi.org/10.1212/wnl.42.10.1859.

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32

Westaway, D., C. Cooper, S. Turner, M. Da Costa, G. A. Carlson, and S. B. Prusiner. "Structure and polymorphism of the mouse prion protein gene." Proceedings of the National Academy of Sciences 91, no. 14 (July 5, 1994): 6418–22. http://dx.doi.org/10.1073/pnas.91.14.6418.

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Laplanche, Jean-Louis, Jacqueline Chatelain, Jean-Marie Launay, Claire Gazengel, and Michel Vidaud. "Deletion in prion protein gene in a Moroccan family." Nucleic Acids Research 18, no. 22 (1990): 6745. http://dx.doi.org/10.1093/nar/18.22.6745.

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34

Zhao, Hui, Xiao-Yan Wang, Wei Zou, and Ya-Ping Zhang. "Prion protein gene (PRNP) polymorphisms in native Chinese cattle." Genome 53, no. 2 (February 2010): 138–45. http://dx.doi.org/10.1139/g09-087.

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Polymorphisms in four regions of the bovine prion protein gene (PRNP) confer susceptibility to bovine spongiform encephalopathy (BSE). These polymorphisms include a 23-bp insertion/deletion (indel) in the promoter region, a 12-bp indel in intron 1, an octapeptide repeat or 24-bp indel in the open reading frame, and a single nucleotide polymorphism (SNP) in the coding region. In this study, we investigated the frequency distributions of genotypes, alleles, and haplotypes at these indel sites in 349 native Chinese cattle and sequence variants in 50 samples. Our results showed that cattle in southern China have low frequencies of the 12-bp deletion allele and the 23-bp deletion / 12-bp deletion haplotype, which have been suggested to be relevant to BSE susceptibility. Interestingly, a significant difference was observed between BSE-affected cattle and healthy Chinese cattle in the 12-bp indel polymorphism. A total of 14 SNPs were discovered in the coding region of PRNP in Chinese cattle. Three of these SNPs were associated with amino acid changes (K3T, P54S, and S154N). The E211K substitution that was recently reported in the US atypical BSE case was not detected in this study.

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35

O’DOHERTY, E., M. AHERNE, S. ENNIS, E. WEAVERS, J. F. ROCHE, and T. SWEENEY. "Prion protein gene polymorphisms in pedigree sheep in Ireland." Research in Veterinary Science 70, no. 1 (February 2001): 51–56. http://dx.doi.org/10.1053/rvsc.2000.0441.

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Owen, Frank, Mark Poulter, John Collinge, Martin Leach, Tarulata Shah, Raymond Lofthouse, Yanfang Chen, et al. "Insertions in the prion protein gene in atypical dementias." Experimental Neurology 112, no. 2 (May 1991): 240–42. http://dx.doi.org/10.1016/0014-4886(91)90075-n.

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MEYDAN, HASAN, ERKAN PEHLİVAN, MUSTAFA MUHIP ÖZKAN, MEHMET ALI YILDIZ, and WILFRED GOLDMANN. "Prion protein gene polymorphisms in Turkish native goat breeds." Journal of Genetics 96, no. 2 (May 18, 2017): 299–305. http://dx.doi.org/10.1007/s12041-017-0763-1.

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Yamada, M., S. Satoh, N. Sodeyama, H. Fujigasaki, K. Kaneko, Y. Wada, Y. Itoh, and M. Matsushita. "Spastic paraparesis and mutations in the prion protein gene." Journal of the Neurological Sciences 134, no. 1-2 (December 1995): 215–16. http://dx.doi.org/10.1016/0022-510x(95)00250-4.

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39

Abdel-Aziem, Sekena H., Heba A. M. Abd El-Kader, Sally S. Alam, Omaima M. Abd El-Moneim, and Othman E. Othman. "Nucleotide structure of prion protein gene in Egyptian camels." Journal of Applied Animal Research 47, no. 1 (January 1, 2019): 123–28. http://dx.doi.org/10.1080/09712119.2019.1580584.

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40

Dlouhy, S., Y. Feng, K. Young, T. Bird, C. DeCarli, M. E. Hodes, P. Piccardo, and B. Ghetti. "AN INTRON MUTATION IN THE PRION PROTEIN GENE (PRNP)." Journal of Neuropathology and Experimental Neurology 58, no. 5 (May 1999): 550. http://dx.doi.org/10.1097/00005072-199905000-00176.

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41

Zimmermann, Klaus, Peter L. Turecek, and Hans Peter Schwarz. "Genotyping of the prion protein gene at codon 129." Acta Neuropathologica 97, no. 4 (April 4, 1999): 355–58. http://dx.doi.org/10.1007/s004010050998.

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42

Kim, Yong-Chan, and Byung-Hoon Jeong. "First report of prion-related protein gene (PRNT) polymorphisms in cattle." Veterinary Record 182, no. 25 (April 17, 2018): 717. http://dx.doi.org/10.1136/vr.104123.

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Prion diseases are caused by structural changes in normal prion protein (PrPC). The prion gene family includes four members: prion protein (PRNP), prion-like protein (PRND), shadow of PRNP (SPRN) and prion-related protein (PRNT). Genetic association studies of prion diseases and the other genes in the prion gene family, except for PRNT, have been performed in cattle. Our previous studies indicated that the distribution of PRNP promoter polymorphisms related with bovine spongiform encephalopathy susceptibility is significantly different in Hanwoo (Korean native cattle) and Holstein cattle. However, PRNT polymorphisms have not been reported thus far in cattle. Hence, we examined the PRNT single nucleotide polymorphisms (SNPs) in 315 Hanwoo and 140 Holstein cattle. We found a total of two SNPs, PRNT c.-87C>T and PRNT c.-37G>C, in the 5’ untranslated region of exon 2. The c.-87C>T and c.-37G>C genotype (P<0.0001) and allele (P<0.0001) frequencies exhibited significant differences in the distribution between Hanwoo and Holstein cattle. In addition, the c.-37G<C polymorphism was not found in Hanwoo. Interestingly, we did not find any polymorphisms in the ORF of bovine PRNT, which is in contrast with the highly polymorphic ovine PRNT ORF region. This is the first genetic research of the PRNT gene in cattle.

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Won, Sae-Young, Yong-Chan Kim, Kyoungtag Do, and Byung-Hoon Jeong. "Absence of Strong Genetic Linkage Disequilibrium between Single Nucleotide Polymorphisms (SNPs) in the Prion Protein Gene (PRNP) and the Prion-Like Protein Gene (PRND) in the Horse, a Prion-Resistant Species." Genes 11, no. 5 (May 7, 2020): 518. http://dx.doi.org/10.3390/genes11050518.

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Prion disease is a fatal neurodegenerative disorder caused by a deleterious prion protein (PrPSc). However, prion disease has not been reported in horses during outbreaks of transmissible spongiform encephalopathies (TSEs) in various animals in the UK. In previous studies, single nucleotide polymorphisms (SNPs) in the prion protein gene (PRNP) have been significantly associated with susceptibility to prion disease, and strong linkage disequilibrium (LD) between PRNP and prion-like protein gene (PRND) SNPs has been identified in prion disease-susceptible species. On the other hand, weak LD values have been reported in dogs, a prion disease-resistant species. In this study, we investigated SNPs in the PRND gene and measured the LD values between the PRNP and PRND SNPs and the impact of a nonsynonymous SNP found in the horse PRND gene. To identify SNPs in the PRND gene, we performed direct sequencing of the PRND gene. In addition, to assess whether the weak LD value between the PRNP and PRND SNPs is a characteristic of prion disease-resistant animals, we measured the LD value between the PRNP and PRND SNPs using D’ and r2 values. Furthermore, we evaluated the impact of a nonsynonymous SNP in the Doppel protein with PolyPhen-2, PROVEAN, and PANTHER. We observed two novel SNPs, c.331G > A (A111T) and c.411G > C. The genotype and allele frequencies of the c.331G > A (A111T) and c.411G > C SNPs were significantly different between Jeju, Halla, and Thoroughbred horses. In addition, we found a total of three haplotypes: GG, AG, and GC. The GG haplotype was the most frequently observed in Jeju and Halla horses. Furthermore, the impact of A111T on the Doppel protein was predicted to be benign by PolyPhen-2, PROVEAN, and PANTHER. Interestingly, a weak LD value between the PRNP and PRND SNPs was found in the horse, a prion disease-resistant animal. To the best of our knowledge, these results suggest that a weak LD value could be one feature of prion disease-resistant animals.

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Kim, Yong-Chan, and Byung-Hoon Jeong. "The first report of prion-related protein gene (PRNT) polymorphisms in goat." Acta Veterinaria Hungarica 65, no. 2 (June 2017): 291–300. http://dx.doi.org/10.1556/004.2017.028.

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Prion protein is encoded by the prion protein gene (PRNP). Polymorphisms of several members of the prion gene family have shown association with prion diseases in several species. Recent studies on a novel member of the prion gene family in rams have shown that prion-related protein gene (PRNT) has a linkage with codon 26 of prion-like protein (PRND). In a previous study, codon 26 polymorphism of PRND has shown connection with PRNP haplotype which is strongly associated with scrapie vulnerability. In addition, the genotype of a single nucleotide polymorphism (SNP) at codon 26 of PRND is related to fertilisation capacity. These findings necessitate studies on the SNP of PRNT gene which is connected with PRND. In goat, several polymorphism studies have been performed for PRNP, PRND, and shadow of prion protein gene (SPRN). However, polymorphism on PRNT has not been reported. Hence, the objective of this study was to determine the genotype and allelic distribution of SNPs of PRNT in 238 Korean native goats and compare PRNT DNA sequences between Korean native goats and several ruminant species. A total of five SNPs, including PRNT c.-114G > T, PRNT c.-58A > G in the upstream of PRNT gene, PRNT c.71C > T (p.Ala24Val) and PRNT c.102G > A in the open reading frame (ORF) and c.321C > T in the downstream of PRNT gene, were found in this study. All five SNPs of caprine PRNT gene in Korean native goat are in complete linkage disequilibrium (LD) with a D’ value of 1.0. Interestingly, comparative sequence analysis of the PRNT gene revealed five mismatches between DNA sequences of Korean native goats and those of goats deposited in the GenBank. Korean native black goats also showed 5 mismatches in PRNT ORF with cattle. To the best of our knowledge, this is the first genetic research of the PRNT gene in goat.

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Sisó, Sílvia, Lorenzo González, and Martin Jeffrey. "Neuroinvasion in Prion Diseases: The Roles of Ascending Neural Infection and Blood Dissemination." Interdisciplinary Perspectives on Infectious Diseases 2010 (2010): 1–16. http://dx.doi.org/10.1155/2010/747892.

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Prion disorders are infectious, neurodegenerative diseases that affect humans and animals. Susceptibility to some prion diseases such as kuru or the new variant of Creutzfeldt-Jakob disease in humans and scrapie in sheep and goats is influenced by polymorphisms of the coding region of the prion protein gene, while other prion disorders such as fatal familial insomnia, familial Creutzfeldt-Jakob disease, or Gerstmann-Straussler-Scheinker disease in humans have an underlying inherited genetic basis. Several prion strains have been demonstrated experimentally in rodents and sheep. The progression and pathogenesis of disease is influenced by both genetic differences in the prion protein and prion strain. Some prion diseases only affect the central nervous system whereas others involve the peripheral organs prior to neuroinvasion. Many experiments undertaken in different species and using different prion strains have postulated common pathways of neuroinvasion. It is suggested that prions access the autonomic nerves innervating peripheral organs and tissues to finally reach the central nervous system. We review here published data supporting this view and additional data suggesting that neuroinvasion may concurrently or independently involve the blood vascular system.

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46

Ganusova, Elena E., Laura N. Ozolins, Srishti Bhagat, Gary P. Newnam, Renee D. Wegrzyn, Michael Y. Sherman, and Yury O. Chernoff. "Modulation of Prion Formation, Aggregation, and Toxicity by the Actin Cytoskeleton in Yeast." Molecular and Cellular Biology 26, no. 2 (January 15, 2006): 617–29. http://dx.doi.org/10.1128/mcb.26.2.617-629.2006.

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ABSTRACT Self-perpetuating protein aggregates transmit prion diseases in mammals and heritable traits in yeast. De novo prion formation can be induced by transient overproduction of the corresponding prion-forming protein or its prion domain. Here, we demonstrate that the yeast prion protein Sup35 interacts with various proteins of the actin cortical cytoskeleton that are involved in endocytosis. Sup35-derived aggregates, generated in the process of prion induction, are associated with the components of the endocytic/vacuolar pathway. Mutational alterations of the cortical actin cytoskeleton decrease aggregation of overproduced Sup35 and de novo prion induction and increase prion-related toxicity in yeast. Deletion of the gene coding for the actin assembly protein Sla2 is lethal in cells containing the prion isoforms of both Sup35 and Rnq1 proteins simultaneously. Our data are consistent with a model in which cytoskeletal structures provide a scaffold for generation of large aggregates, resembling mammalian aggresomes. These aggregates promote prion formation. Moreover, it appears that the actin cytoskeleton also plays a certain role in counteracting the toxicity of the overproduced potentially aggregating proteins.

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Campana, Vincenza, Lorena Zentilin, Ilaria Mirabile, Agata Kranjc, Philippe Casanova, Mauro Giacca, Stanley B. Prusiner, Giuseppe Legname, and Chiara Zurzolo. "Development of antibody fragments for immunotherapy of prion diseases." Biochemical Journal 418, no. 3 (February 25, 2009): 507–15. http://dx.doi.org/10.1042/bj20081541.

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Prions are infectious proteins responsible for a group of fatal neurodegenerative diseases called TSEs (transmissible spongiform encephalopathies) or prion diseases. In mammals, prions reproduce themselves by recruiting the normal cellular protein PrPC and inducing its conversion into the disease-causing isoform denominated PrPSc. Recently, anti-prion antibodies have been shown to permanently cure prion-infected cells. However, the inability of full-length antibodies and proteins to cross the BBB (blood-brain barrier) hampers their use in the therapy of TSEs in vivo. Alternatively, brain delivery of prion-specific scFv (single-chain variable fragment) by AAV (adeno-associated virus) transfer delays the onset of the disease in infected mice, although protection is not complete. We investigated the anti-prion effects of a recombinant anti-PrP (D18) scFv by direct addition to scrapie-infected cell cultures or by infection with both lentivirus and AAV-transducing vectors. We show that recombinant anti-PrP scFv is able to reduce proteinase K-resistant PrP content in infected cells. In addition, we demonstrate that lentiviruses are more efficient than AAV in gene transfer of the anti-PrP scFv gene and in reducing PrPSc content in infected neuronal cell lines. Finally, we have used a bioinformatic approach to construct a structural model of the D18scFv–PrPC complex. Interestingly, according to the docking results, ArgPrP151 (Arg151 from prion protein) is the key residue for the interactions with D18scFv, anchoring the PrPC to the cavity of the antibody. Taken together, these results indicate that combined passive and active immunotherapy targeting PrP might be promising strategies for therapeutic intervention in prion diseases.

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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 (November 18, 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 virus (IAV) induced the conversion of PrPC into PrPSc as well as formation of infectious prions in mouse neuroblastoma cells after infection, suggesting the causative role of the neuronal infection of IAV in sporadic prion diseases. Here, we discuss the conversion mechanism of PrPC into PrPSc in different types of prion diseases, by presenting our findings of the IAV infection-induced conversion of PrPC into PrPSc and by reviewing the so far reported transgenic animal models of hereditary prion diseases and the reverse genetic studies, which have revealed the structure-function relationship for PrPC to convert into PrPSc after prion infection.

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Ayers, Jacob I., Nick A. Paras, and Stanley B. Prusiner. "Expanding spectrum of prion diseases." Emerging Topics in Life Sciences 4, no. 2 (August 17, 2020): 155–67. http://dx.doi.org/10.1042/etls20200037.

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Prions were initially discovered in studies of scrapie, a transmissible neurodegenerative disease (ND) of sheep and goats thought to be caused by slow viruses. Once scrapie was transmitted to rodents, it was discovered that the scrapie pathogen resisted inactivation by procedures that modify nucleic acids. Eventually, this novel pathogen proved to be a protein of 209 amino acids, which is encoded by a chromosomal gene. After the absence of a nucleic acid within the scrapie agent was established, the mechanism of infectivity posed a conundrum and eliminated a hypothetical virus. Subsequently, the infectious scrapie prion protein (PrPSc) enriched for β-sheet was found to be generated from the cellular prion protein (PrPC) that is predominantly α-helical. The post-translational process that features in nascent prion formation involves a templated conformational change in PrPC that results in an infectious copy of PrPSc. Thus, prions are proteins that adopt alternative conformations, which are self-propagating and found in organisms ranging from yeast to humans. Prions have been found in both Alzheimer's (AD) and Parkinson's (PD) diseases. Mutations in APP and α-synuclein genes have been shown to cause familial AD and PD. Recently, AD was found to be a double prion disorder: both Aβ and tau prions feature in this ND. Increasing evidence argues for α-synuclein prions as the cause of PD, multiple system atrophy, and Lewy body dementia.

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Kovacs, G. G. "Inherited prion disease with A117V mutation of the prion protein gene: a novel Hungarian family." Journal of Neurology, Neurosurgery & Psychiatry 70, no. 6 (June 1, 2001): 802–5. http://dx.doi.org/10.1136/jnnp.70.6.802.

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