Special Issue "Prions"

Guest Editor
Dr. Wen-Quan Zou
Associate Professor of Departments of Pathology and Neurology, Associate Director of National Prion Disease Pathology Surveillance Center, Case Western Reserve University School of Medicine, Adelbert Road, Room 403, Cleveland, OH 44106, USA
Website: http://www.case.edu/med/pathology/faculty/zou.html
E-Mail: Wenquan.zou@case.edu
Phone: +1 216 368 8993
Fax: +1 216 368 2546
Interests: prions; prion diseases; neurodegenerative disorders; protein misfolding disorders; protein aggregations; neuroscience; alzheimer’s disease; and glycosylation

Guest Editor
Prof. Dr. Xiao-Ping Dong
Director of Prion Research Group, State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Changbai Rd 155, Beijing 102206, People's Republic of China
E-Mail: dongxp238@sina.com
Phone: +86 10 58900815
Fax: +86 10 58900815
Interests: prions; prion diseases

Guest Editor
Prof. Dr. Yong-Sun Kim
Professor of Department of Microbiology and Immunology, College of Medicine, Director of Ilsong Institute of Life Science, Executive Vice President for Health & Biomedical Sciences, Hallym University, 1605-4, Gwanyang-dong, Dongan-gu, Anyang, Gyeonggi-do 431-060, Korea
Website: http://english.hallym.ac.kr/ilsong_science/index.html
E-Mail: yskim@hallym.ac.kr
Phone: +82 31 381 0972
Fax: +82 31 388 3427
Interests: prion diseases; endogenous retrovirus; oxidative stress; protein citrullination; autophagy and neurodegenerative disorders

Dear Colleagues,

Prions are infectious proteinaceous pathogens responsible for a group of fatal transmissible spongiform encephalopathies or prion diseases in animals and humans. An infectious scrapie form of prion protein (termed PrPSc) is the only known component in prions. PrPSc is derived from the cellular PrP (PrPC) through a conformational transition triggered by PrP mutation, exogenous PrPSc infection, or unknown reasons. Animal prion diseases mainly include scrapie, bovine spongiform encephalopathy, and chronic wasting disease, whereas human prion diseases include Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker disease, fatal familial insomnia, kuru, and variably protease-sensitive prionopathy. Unlike other infectious agents such as bacteria, viruses, and fungi, which contain genomes composed of either DNA or RNA, prions may be the only known infectious pathogens that are devoid of nucleic acids. Although prion diseases are rare, it is crucial to keep updated on the development of prions because of the unique properties of prions, no cure for prion diseases yet, and their potential for renewed outbreaks of disease in animals, humans, or both.

Both original research and review articles focusing on molecular mechanisms underlying the prion formation and pathogenesis of prion diseases are welcomed. Especially, we seek manuscripts that report emerging atypical prions and prion diseases as well as innovative strategies and methods for the determination of prions and treatment of prion diseases. Potential topics include, but are not limited to:

• Atypical prions and prion diseases
• Prion-like mechanisms in other diseases
• Co-factors in prion formation
• Diagnostic assays
• Strategies for development of vaccination and treatment

We look forward to your contributions and to a valuable edition that will promote further developments in this exciting field.
Thank you for your collaboration.

Wen-Quan Zou, MD, PhD
Xiao-Ping Dong, MD, PhD
Yong-Sun Kim, MD, PhD
Guest Editors

Submission

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• prions
• prion diseases
• prion formation
• scrapie
• bovine spongiform encephalopathy
• chronic wasting disease
• creutzfeldt-Jakob disease
• Gerstmann-Sträussler-Scheinker disease
• variably protease-sensitive prionopathy
• glycosylation
• mutation
• virus
• oxidative stress
• insoluble prion protein
• redox
• diagnosis
• vaccine
• therapeutics

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	p. 149-163 Open Access Review Review: Prions and Prion-Like Pathogens in Neurodegenerative Disorders by Caterina Peggion, Maria Catia Sorgato and Alessandro Bertoli Pathogens 2014, 3(1), 149-163; doi:10.3390/pathogens3010149 Received: 10 January 2014 / Revised: 24 January 2014 / Accepted: 1 February 2014 / Published: 18 February 2014 Show/Hide Abstract | PDF Full-text (234 KB) | HTML Full-text | XML Full-text Abstract: Prions are unique elements in biology, being able to transmit biological information from one organism to another in the absence of nucleic acids. They have been identified as self-replicating proteinaceous agents responsible for the onset of rare and fatal neurodegenerative disorders—known as transmissible spongiform encephalopathies, or prion diseases—which affect humans and other animal species. More recently, it has been proposed that other proteins associated with common neurodegenerative disorders, such as Alzheimer’s and Parkinson’s disease, can self-replicate like prions, thus sustaining the spread of neurotoxic entities throughout the nervous system. Here, we review findings that have contributed to expand the prion concept, and discuss if the involved toxic species can be considered bona fide prions, including the capacity to infect other organisms, or whether these pathogenic aggregates share with prions only the capability to self-replicate. (This article belongs to the Special Issue Prions)
	p. 533-543 Open Access Review Review: Involvement of Endogenous Retroviruses in Prion Diseases by Yun-Jung Lee, Byung-Hoon Jeong, Eun-Kyung Choi and Yong-Sun Kim Pathogens 2013, 2(3), 533-543; doi:10.3390/pathogens2030533 Received: 8 June 2013 / Revised: 25 July 2013 / Accepted: 9 August 2013 / Published: 12 August 2013 Show/Hide Abstract | Cited by 2 | PDF Full-text (198 KB) | HTML Full-text | XML Full-text Abstract: For millions of years, vertebrates have been continuously exposed to infection by retroviruses. Ancient retroviral infection of germline cells resulted in the formation and accumulation of inherited retrovirus sequences in host genomes. These inherited retroviruses are referred to as endogenous retroviruses (ERVs), and recent estimates have revealed that a significant portion of animal genomes is made up of ERVs. Although various host factors have suppressed ERV activation, both positive and negative functions have been reported for some ERVs in normal and abnormal physiological conditions, such as in disease states. Similar to other complex diseases, ERV activation has been observed in prion diseases, and this review will discuss the potential involvement of ERVs in prion diseases. (This article belongs to the Special Issue Prions)
	p. 520-532 Open Access Article: Evaluation of the Zoonotic Potential of Transmissible Mink Encephalopathy by Emmanuel E. Comoy, Jacqueline Mikol, Marie-Madeleine Ruchoux, Valérie Durand, Sophie Luccantoni-Freire, Capucine Dehen, Evelyne Correia, Cristina Casalone, Juergen A. Richt, Justin J. Greenlee, Juan Maria Torres, Paul Brown and Jean-Philippe Deslys Pathogens 2013, 2(3), 520-532; doi:10.3390/pathogens2030520 Received: 27 June 2013 / Revised: 28 July 2013 / Accepted: 30 July 2013 / Published: 30 July 2013 Show/Hide Abstract | PDF Full-text (481 KB) | HTML Full-text | XML Full-text Abstract: Successful transmission of Transmissible Mink Encephalopathy (TME) to cattle supports the bovine hypothesis for the still controversial origin of TME outbreaks. Human and primate susceptibility to classical Bovine Spongiform Encephalopathy (c-BSE) and the transmissibility of L-type BSE to macaques indicate a low cattle-to-primate species barrier. We therefore evaluated the zoonotic potential of cattle-adapted TME. In less than two years, this strain induced in cynomolgus macaques a neurological disease similar to L-BSE but distinct from c-BSE. TME derived from another donor species (raccoon) induced a similar disease with even shorter incubation periods. L-BSE and cattle-adapted TME were also transmissible to transgenic mice expressing human prion protein (PrP). Secondary transmissions to transgenic mice expressing bovine PrP maintained the features of the three tested bovine strains (cattle TME, c-BSE and L-BSE) regardless of intermediate host. Thus, TME is the third animal prion strain transmissible to both macaques and humanized transgenic mice, suggesting zoonotic potentials that should be considered in the risk analysis of animal prion diseases for human health. Moreover, the similarities between TME and L-BSE are highly suggestive of a link between these strains, and therefore the possible presence of L-BSE for many decades prior to its identification in USA and Europe. (This article belongs to the Special Issue Prions)
	p. 506-519 Open Access Article: Curcumin Reduces Amyloid Fibrillation of Prion Protein and Decreases Reactive Oxidative Stress by Chi-Fen Lin, Kun-Hua Yu, Cheng-Ping Jheng, Raymond Chung and Cheng-I Lee Pathogens 2013, 2(3), 506-519; doi:10.3390/pathogens2030506 Received: 10 July 2013 / Revised: 17 July 2013 / Accepted: 21 July 2013 / Published: 25 July 2013 Show/Hide Abstract | PDF Full-text (1104 KB) | HTML Full-text | XML Full-text Abstract: Misfolding and aggregation into amyloids of the prion protein (PrP) is responsible for the development of fatal transmissible neurodegenerative diseases. Various studies on curcumin demonstrate promise for the prevention of Alzheimer’s disease and inhibition of PrPres accumulation. To evaluate the effect of curcumin on amyloid fibrillation of prion protein, we first investigated the effect of curcumin on mouse prion protein (mPrP) in a cell-free system. Curcumin reduced the prion fibril formation significantly. Furthermore, we monitored the change in apoptosis and reactive oxygen species (ROS) level upon curcumin treatment in mouse neuroblastoma cells (N2a). Curcumin effectively rescues the cells from apoptosis and decreases the ROS level caused by subsequent co-incubation with prion amyloid fibrils. The assays in cell-free mPrP and in N2a cells of this work verified the promising effect of curcumin on the prevention of transmissible neurodegenerative diseases. (This article belongs to the Special Issue Prions)
	p. 472-505 Open Access Review Review: Kuru: A Journey Back in Time from Papua New Guinea to the Neanderthals’ Extinction by Pawel P. Liberski Pathogens 2013, 2(3), 472-505; doi:10.3390/pathogens2030472 Received: 19 June 2013 / Revised: 4 July 2013 / Accepted: 12 July 2013 / Published: 18 July 2013 Show/Hide Abstract | PDF Full-text (2466 KB) | HTML Full-text | XML Full-text Abstract: Kuru, the first human transmissible spongiform encephalopathy was transmitted to chimpanzees by D. Carleton Gajdusek (1923–2008). In this review, I briefly summarize the history of this seminal discovery along its epidemiology, clinical picture, neuropathology and molecular genetics. The discovery of kuru opened new windows into the realms of human medicine and was instrumental in the later transmission of Creutzfeldt-Jakob disease and Gerstmann-Sträussler-Scheinker disease as well as the relevance that bovine spongiform encephalopathy had for transmission to humans. The transmission of kuru was one of the greatest contributions to biomedical sciences of the 20th century. (This article belongs to the Special Issue Prions)
	p. 457-471 Open Access Review Review: Prions in Variably Protease-Sensitive Prionopathy: An Update by Wen-Quan Zou, Pierluigi Gambetti, Xiangzhu Xiao, Jue Yuan, Jan Langeveld and Laura Pirisinu Pathogens 2013, 2(3), 457-471; doi:10.3390/pathogens2030457 Received: 12 June 2013 / Revised: 28 June 2013 / Accepted: 2 July 2013 / Published: 5 July 2013 Show/Hide Abstract | Cited by 1 | PDF Full-text (353 KB) | HTML Full-text | XML Full-text Abstract: Human prion diseases, including sporadic, familial, and acquired forms such as Creutzfeldt-Jakob disease (CJD), are caused by prions in which an abnormal prion protein (PrPSc) derived from its normal cellular isoform (PrPC) is the only known component. The recently-identified variably protease-sensitive prionopathy (VPSPr) is characterized not only by an atypical clinical phenotype and neuropathology but also by the deposition in the brain of a peculiar PrPSc. Like other forms of human prion disease, the pathogenesis of VPSPr also currently remains unclear. However, the findings of the peculiar features of prions from VPSPr and of the possible association of VPSPr with a known genetic prion disease linked with a valine to isoleucine mutation at residue 180 of PrP reported recently, may be of great importance in enhancing our understanding of not only this atypical human prion disease in particular, but also other prion diseases in general. In this review, we highlight the physicochemical and biological properties of prions from VPSPr and discuss the pathogenesis of VPSPr including the origin and formation of the peculiar prions. (This article belongs to the Special Issue Prions)
	p. 446-456 Open Access Article: Biochemical Characterization of Prion Strains in Bank Voles by Laura Pirisinu, Stefano Marcon, Michele Angelo Di Bari, Claudia D'Agostino, Umberto Agrimi and Romolo Nonno Pathogens 2013, 2(3), 446-456; doi:10.3390/pathogens2030446 Received: 22 May 2013 / Revised: 25 June 2013 / Accepted: 26 June 2013 / Published: 2 July 2013 Show/Hide Abstract | Cited by 1 | PDF Full-text (321 KB) | HTML Full-text | XML Full-text Abstract: Prions exist as different strains exhibiting distinct disease phenotypes. Currently, the identification of prion strains is still based on biological strain typing in rodents. However, it has been shown that prion strains may be associated with distinct PrPSc biochemical types. Taking advantage of the availability of several prion strains adapted to a novel rodent model, the bank vole, we investigated if any prion strain was actually associated with distinctive PrPSc biochemical characteristics and if it was possible to univocally identify strains through PrPSc biochemical phenotypes. We selected six different vole-adapted strains (three human-derived and three animal-derived) and analyzed PrPSc from individual voles by epitope mapping of protease resistant core of PrPSc (PrPres) and by conformational stability and solubility assay. Overall, we discriminated five out of six prion strains, while two different scrapie strains showed identical PrPSc types. Our results suggest that the biochemical strain typing approach here proposed was highly discriminative, although by itself it did not allow us to identify all prion strains analyzed. (This article belongs to the Special Issue Prions)
	p. 436-445 Open Access Review Review: The Functional Role of Prion Protein (PrPC) on Autophagy by Hae-Young Shin, Jae-Min Oh and Yong-Sun Kim Pathogens 2013, 2(3), 436-445; doi:10.3390/pathogens2030436 Received: 2 May 2013 / Revised: 11 June 2013 / Accepted: 18 June 2013 / Published: 26 June 2013 Show/Hide Abstract | PDF Full-text (351 KB) | HTML Full-text | XML Full-text Abstract: Cellular prion protein (PrPC) plays an important role in the cellular defense against oxidative stress. However, the exact protective mechanism of PrPC is unclear. Autophagy is essential for survival, differentiation, development, and homeostasis in several organisms. Although the role that autophagy plays in neurodegenerative disease has yet to be established, it is clear that autophagy-induced cell death is observed in neurodegenerative disorders that exhibit protein aggregations. Moreover, autophagy can promote cell survival and cell death under various conditions. In this review, we describe the involvement of autophagy in prion disease and the effects of PrPC. (This article belongs to the Special Issue Prions)
	p. 92-104 Open Access Article: Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain by Kazuo Kasai, Yoshifumi Iwamaru, Kentaro Masujin, Morikazu Imamura, Shirou Mohri and Takashi Yokoyama Pathogens 2013, 2(1), 92-104; doi:10.3390/pathogens2010092 Received: 9 January 2013 / Revised: 7 February 2013 / Accepted: 9 February 2013 / Published: 18 February 2013 Show/Hide Abstract | PDF Full-text (1728 KB) | HTML Full-text | XML Full-text Abstract: The pathological prion protein, PrPSc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrPSc aggregates of mouse-adapted prion strains. We showed that small PrPSc aggregates, previously thought to be PK-sensitive, are resistant to PK digestion. Furthermore, we showed that small PrPSc aggregates of the Chandler scrapie strain have greater resistance to PK digestion and aggregation-denaturation than large PrPSc aggregates of this strain. We conclude that this strain consists of heterogeneous PrPSc. (This article belongs to the Special Issue Prions)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Last update: 6 February 2013