• Journal of Microbiology and Biotechnology
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• 제17권7호
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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.

• 한국수산과학회지
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• 제47권4호
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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.

• Journal of Microbiology and Biotechnology
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• 제26권9호
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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.

• BMB Reports
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• 제40권5호
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• pp.662-669
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• 2007

Although the function of cellular prion protein (PrP$^C$) and the pathogenesis of prion diseases have been widely described, the mechanisms are not fully clarified. In this study, increases of the portion of non-glycosylated prion protein deposited in the hamster brains infected with scrapie strain 263K were described. To elucidate the pathological role of glycosylation profile of PrP, wild type human PrP (HuPrP) and two genetic engineering generated non-glycosylated PrP mutants (N181Q/N197Q and T183A/T199A) were transiently expressed in human astrocytoma cell line SF126. The results revealed that expressions of non-glycosylated PrP induced significantly more apoptosis cells than that of wild type PrP. It illustrated that Bcl-2 proteins might be involved in the apoptosis pathway of non-glycosylated PrPs. Our data highlights that removal of glycosylation of prion protein provokes cells apoptosis.

• Bulletin of the Korean Chemical Society
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• 제32권10호
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• pp.3553-3554
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• 2011

• BMB Reports
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• 제56권12호
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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.

• 공업화학
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• 제20권6호
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• pp.628-631
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• 2009

최근 광우병 파동과 프리온 단백질의 전염으로 인하여 발생되는 것으로 알려진 크로이츠펠트 야콥병에 대하여 폭넓게 연구되면서 생화학계에서 프리온 단백질에 대한 관심은 상당하다. 본 연구에서는 프리온 단백질의 일부분인 PrP 106-126의 마이크로 몰농도 단위의 정량분석을 실시하였다. 본 연구에서 플로래스카민은 일차 아민과 반응하여 형광을 띠는 물질로써, 알파이미저는 형광의 세기를 측정하는 기기로써 사용되었다. 따라서 합성된 PrP 106-126으로 플로래스카민과 알파이미저를 이용하여 마이크로 몰농도단위의 정량 분석을 위한 조건을 정립하였으며 이를 통하여 표준곡선을 얻을 수 있었다. 이 방법은 차후 변형 프리온 단백질에 대한 응집저해제 및 의약품 연구에 큰 기여를 할 것이다.

• 대한영상의학회지
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• 제84권3호
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• pp.745-749
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• 2023

Gerstmann-Strssler-Scheinker (이하 GSS) disease는 드문 유전성 프라이온 질환으로 초기에 발생해 진행하는 소뇌실조와 후기에 발생하는 인지기능 저하가 특징적이다. 저자들은 진행하는 보행장애와 5개월 후 발생한 구음 장애, 인지 기능 저하를 주소로 내원한 39세 남성 환자의 증례를 보고하고자 한다. 뇌 MRI에서 양측 대뇌피질과 기저핵, 시상에 확산 저하를 동반한 T2 강조영상에서의 고신호 강도 병변이 관찰되었다. 환자는 모두 40-50대에 비슷한 증상을 호소하였던 가족력을 동반하였으며 PRNP 유전자 검사를 통해 GSS로 확진되었다.

• BMB Reports
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• 제42권7호
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• pp.444-449
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• 2009

Different neurodegenerative disorders like prion disease, is caused by protein misfolding conformers. Reverse-transfected cytosolic prion protein (PrP) and PrP expressed in the cytosol have been shown to be neurotoxic. To investigate the possible mechanism of neurotoxicity due to accumulation of PrP in cytosol, a PrP mutant lacking the signal and GPI (CytoPrP) was introduced into the SH-SY5Y cell. MTT and trypan blue assays indicated that the viability of cells expressing CytoPrP was remarkably reduced after treatment of MG-132. Obvious apoptosis phenomena were detected in the cells accumulated with CytoPrP, including loss of mitochondrial transmembrane potential, increase of caspase-3 activity, more annexin V/PI-double positive-stained cells and reduced Bcl-2 level. Moreover, DNA fragmentation and TUNEL assays also revealed clear evidences of late apoptosis in the cells accumulated CytoPrP. These data suggest that the accumulation of CytoPrP in cytoplasm may trigger cell apoptosis, in which mitochondrial relative apoptosis pathway seems to play critical role.

• EDISON SW 활용 경진대회 논문집
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• 제6회(2017년)
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• pp.32-38
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• 2017

Prion is a group of the proteins known for its infection mechanisms of Creutzfeldt-Jakob disease (CJD) and other diseases. Solved structures and proven biological roles of fungal prions add tremendous potential to conducting computational simulations. Our research focuses on the binding dynamics of HET-s(218-289), one of the heterokaryon fungal prion originated from Podospora anserina, by calculating the binding free energy using umbrella sampling at 300 K. The binding free energy calculated was $-54.5kcal\;mol^{-1}$, relatively similar to the binding energy of other amyloid fibrils. The simulation result suggests the thermodynamic properties of ${\beta}$-solenoid of HET-s prion and its similarity in dissociation pathways compared to amyloids.