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Pathogens
Special Issues
Prions
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Prions

A special issue of Pathogens (ISSN 2076-0817).

Deadline for manuscript submissions: closed (30 April 2013) | Viewed by 102396

Special Issue Editors

Prof. Dr. Wen-Quan Zou

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Guest Editor
1. Distinguished Professor, Director, Institute of Brain Science, Nanchang, China
2. Executive Dean, Jiangxi Academy of Clinical Medical Sciences, Nanchang, China
3. The First Affiliated Hospital of Nanchang University School of Medicine, Nanchang, China
Interests: prions; prion diseases; prion-like; zoonosis; neurodegenerative disorders; protein misfolding disorders; protein aggregations; biomarkers; neuroscience; Alzheimer’s disease; Parkinson’s disease; glycosylation
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Xiao-Ping Dong

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Guest Editor
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
Interests: prions; prion diseases
Prof. Dr. Yong-Sun Kim

E-Mail Website
Guest Editor
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
Interests: prion diseases; endogenous retrovirus; oxidative stress; protein citrullination; autophagy and neurodegenerative disorders

Special Issue Information

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

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Pathogens is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • 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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Published Papers (9 papers)

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Research

Jump to: Review

13 pages, 481 KiB  
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; https://doi.org/10.3390/pathogens2030520 - 30 Jul 2013
Cited by 12 | Viewed by 8265
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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14 pages, 1104 KiB  
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; https://doi.org/10.3390/pathogens2030506 - 25 Jul 2013
Cited by 57 | Viewed by 8536
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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11 pages, 321 KiB  
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; https://doi.org/10.3390/pathogens2030446 - 2 Jul 2013
Cited by 20 | Viewed by 7710
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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13 pages, 1728 KiB  
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; https://doi.org/10.3390/pathogens2010092 - 18 Feb 2013
Cited by 1 | Viewed by 6688
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, [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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Review

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15 pages, 234 KiB  
Review
Prions and Prion-Like Pathogens in Neurodegenerative Disorders
by Caterina Peggion, Maria Catia Sorgato and Alessandro Bertoli
Pathogens 2014, 3(1), 149-163; https://doi.org/10.3390/pathogens3010149 - 18 Feb 2014
Cited by 16 | Viewed by 7187
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
11 pages, 198 KiB  
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; https://doi.org/10.3390/pathogens2030533 - 12 Aug 2013
Cited by 5 | Viewed by 6753
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
34 pages, 2466 KiB  
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; https://doi.org/10.3390/pathogens2030472 - 18 Jul 2013
Cited by 20 | Viewed by 33368
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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15 pages, 353 KiB  
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; https://doi.org/10.3390/pathogens2030457 - 5 Jul 2013
Cited by 23 | Viewed by 12492
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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10 pages, 351 KiB  
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; https://doi.org/10.3390/pathogens2030436 - 26 Jun 2013
Cited by 10 | Viewed by 9871
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Prions)
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