• Journal of Microbiology and Biotechnology
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• v.17 no.7
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• pp.1059-1070
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• 2007

Prion diseases, often called transmissible spongiform encephalopathies (TSEs), are infectious diseases that accompany neurological dysfunctions in many mammalian hosts. Prion diseases include Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (BSE, "mad cow disease") in cattle, scrapie in sheep, and chronic wasting disease (CWD) in deer and elks. The cause of these fatal diseases is a proteinaceous pathogen termed prion that lacks functional nucleic acids. As demonstrated in the BSE outbreak and its transmission to humans, the onset of disease is not limited to a certain species but can be transmissible from one host species to another. Such a striking nature of prions has generated huge concerns in public health and attracted serious attention in the scientific communities. To date, the potential transmission of prions to humans via foodborne infection and iatrogenic routes has not been alleviated. Rather, the possible transmission of human to human or cervids to human aggravates the terrifying situation across the globe. In this review, basic features about prion diseases including clinical and pathological characteristics, etiology, and transmission of diseases are described. Based on recently accumulated evidences, the molecular and biochemical aspects of prions, with an emphasis on the molecular interactions involved in prion conversion that is critical during prion replication and pathogenesis, are also addressed.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.47 no.4
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• pp.341-346
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• 2014

Transmissible spongiform encephalopathies (TSEs), also termed prion diseases, are a threat to food safety and to human and animal health. Variant Creutzfeldt-Jakob disease (vCJD) in humans is caused by the consumption of meat contaminated with bovine spongiform encephalopathy (BSE, mad cow disease). The BSE epidemic in the United Kingdom was shown to be related with the extensive use of BSE-contaminated meat-and-bone meal (MBM) and bovine offal. Many countries worldwide use MBM, as well as meat from cows, for aquaculture feed. This raises concerns about the safety of farmed fish, a major protein source for humans. The present work reviews recent studies on fish prion protein and the transmissibility of mammalian prion agents to fish, providing insights into the future direction of fish prion research.

• Microbiology and Biotechnology Letters
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• v.43 no.2
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• pp.91-96
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• 2015

Prions are proteinaceous infectious particles that cause neurodegenerative diseases, such as scrapie in sheep, bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease (CJD) in humans. Although the detailed process, regarding the abnormal conversion of prion proteins (PrP), remains to be fully elucidated, a number of environmental factors appear to affect the formation of misfolded PrP, termed PrP^Sc. Because oceanic algae contain mycosporine-like amino acids (MAAs), which exhibit cellular defensive activities under a variety of stress conditions, we investigated the level of PrP^Sc in prion-infected neuroblastoma cells using mycosporine-glycine, porphyra-334 and shinorine. When judged by the level of protease-resistant PrP^Sc in western blots, porphyra-334 and shinorine increased the level of PrP^Sc in cells, but mycosporine-glycine did not. The current results indicate that the MAAs tested in this study enhance the formation of PrP^Sc.

• Bulletin of the Korean Chemical Society
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• v.32 no.10
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• pp.3553-3554
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• 2011

• Journal of Microbiology and Biotechnology
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• v.26 no.9
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• pp.1657-1660
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• 2016

Prion diseases are incurable neurodegenerative disorders. Our previous study demonstrated that polylysine was effective in prolonging the incubation period in a rodent model and in alleviating the scrapie prion protein (PrP^Sc) burden in the brain at the terminal stage of the disease. Here, we report that intraperitoneal administration of polylysine suppresses the accumulation of prions in the spleen during the early stages of the disease. This study supports the congruence of PrP^Sc inhibition by polylysine in both the spleen and brain.

• Journal of Microbiology and Biotechnology
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• v.28 no.12
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• pp.2141-2144
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• 2018

Based on previous studies reporting the anti-prion activity of poly-${\text\tiny{L}}$-lysine and poly-${\text\tiny{L}}$-arginine, we investigated cationic poly-${\text\tiny{L}}$-ornithine (PLO), poly-${\text\tiny{L}}$-histidine (PLH), anionic poly-${\text\tiny{L}}$-glutamic acid (PLE) and uncharged poly-${\text\tiny{L}}$-threonine (PLT) in cultured cells chronically infected by prions to determine their anti-prion efficacy. While PLE and PLT did not alter the level of $PrP^{Sc}$, PLO and PLH exhibited potent $PrP^{Sc}$ inhibition in ScN2a cells. These results suggest that the anti-prion activity of poly-basic amino acids is correlated with the cationicity of their functional groups. Comparison of anti-prion activity of PLO and PLH proposes that the anti-prion activity of poly-basic amino acids is associated with their acidic cellular compartments.

• BMB Reports
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• v.56 no.12
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• pp.645-650
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• 2023

Numerous studies have investigated the cellular prion protein (PrP^C) since its discovery. These investigations have explained that its structure is predominantly composed of alpha helices and short beta sheet segments, and when its abnormal scrapie isoform (PrPSc) is infected, PrPSc transforms the PrP^C, leading to prion diseases, including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle. Given its ubiquitous distribution across a variety of cellular types, the PrP^C manifests a diverse range of biological functions, including cell-cell adhesion, neuroprotection, signalings, and oxidative stress response. PrP^C is also expressed in immune tissues, and its functions in these tissues include the activation of immune cells and the formation of secondary lymphoid tissues, such as the spleen and lymph nodes. Moreover, high expression of PrP^C in immune cells plays a crucial role in the pathogenesis of prion diseases. In addition, it affects inflammation and the development and progression of cancer via various mechanisms. In this review, we discuss the studies on the role of PrP^C from various immunological perspectives.

• Proceedings of the Microbiological Society of Korea Conference
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• 2009.05a
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• pp.144-144
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• 2009

• Journal of the Korean Magnetic Resonance Society
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• v.15 no.2
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• pp.175-186
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• 2011

Amyloid fibrils have long been known to be the well known ${\alpha}$-helix to ${\beta}$-sheet transition characterizing the conversion of cellular to scrapie forms of the prion protein. A very short sequence of Yeast prion-like protein, GNNQQNY (SupN), is responsible for aggregation that induces diseases. KSI-fused tandem repeats of SupN vector are constructed and used to express SupN peptide in Escherichia coli (E.Coli). A method for a production, purification, and cleavage of tandem repeats of recombinant isotopically enriched SupN in E. coli is described. This method yields as much as 20 mg/L of isotope-enriched fusion proteins in minimal media. Synthetic SupN peptides and $^{13}C$ Gly labeled SupN peptides are studied by Congo Red staining, Birefringence and transmission electron microscopy to characterize amyloid fibril formation. To get a better understanding of aggregation-structure relationship of 7 residues of Yeast prion-like protein, the change of a conformational structure will be studied by $^{13}C$ solid-state nmr spectroscopy as powder of both amorphous and fibrillar forms.

• Applied Chemistry for Engineering
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• v.20 no.6
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• pp.628-631
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• 2009

Recent social interests on mad cow disease and Creutzfelt-Jacob disease lead researcher' focus onto pathogenic prion proteins causing those diseases. The purpose of this study is to introduce a novel method for micromolecular level quantification of PrP 106-126 peptide, which is a part of prion protein. Fluorescamine has been chosen due to its fluorescence emission characteristics upon reaction with primary amines and Alpha-imager is used to detect the intensity of fluorescence. We succeeded in setting optimal conditions for quantification of PrP 106-206, amyloidogenic prion peptide, at micromolecular level. This study will contribute to identify prion protein aggregation inhibitor and develop new prion protein drug.