Special Issue "Prions"
A special issue of Pathogens (ISSN 2076-0817).
Deadline for manuscript submissions: closed (30 April 2013)
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
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
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
Phone: +86 10 58900815
Fax: +86 10 58900815
Interests: prions; prion diseases
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
Phone: +82 31 381 0972
Fax: +82 31 388 3427
Interests: prion diseases; endogenous retrovirus; oxidative stress; protein citrullination; autophagy and neurodegenerative disorders
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
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a 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 quarterly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. For the first couple of issues the Article Processing Charge (APC) will be waived for well-prepared manuscripts. English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.
- prion diseases
- prion formation
- bovine spongiform encephalopathy
- chronic wasting disease
- creutzfeldt-Jakob disease
- Gerstmann-Sträussler-Scheinker disease
- variably protease-sensitive prionopathy
- oxidative stress
- insoluble prion protein
Pathogens 2014, 3(1), 149-163; doi:10.3390/pathogens3010149
Received: 10 January 2014; in revised form: 24 January 2014 / Accepted: 1 February 2014 / Published: 18 February 2014| PDF Full-text (234 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(3), 533-543; doi:10.3390/pathogens2030533
Received: 8 June 2013; in revised form: 25 July 2013 / Accepted: 9 August 2013 / Published: 12 August 2013| PDF Full-text (198 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(3), 520-532; doi:10.3390/pathogens2030520
Received: 27 June 2013; in revised form: 28 July 2013 / Accepted: 30 July 2013 / Published: 30 July 2013| PDF Full-text (481 KB) | HTML Full-text | XML Full-text
Article: Curcumin Reduces Amyloid Fibrillation of Prion Protein and Decreases Reactive Oxidative Stress
Pathogens 2013, 2(3), 506-519; doi:10.3390/pathogens2030506
Received: 10 July 2013; in revised form: 17 July 2013 / Accepted: 21 July 2013 / Published: 25 July 2013| PDF Full-text (1104 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(3), 472-505; doi:10.3390/pathogens2030472
Received: 19 June 2013; in revised form: 4 July 2013 / Accepted: 12 July 2013 / Published: 18 July 2013| PDF Full-text (2466 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(3), 457-471; doi:10.3390/pathogens2030457
Received: 12 June 2013; in revised form: 28 June 2013 / Accepted: 2 July 2013 / Published: 5 July 2013| PDF Full-text (353 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(3), 446-456; doi:10.3390/pathogens2030446
Received: 22 May 2013; in revised form: 25 June 2013 / Accepted: 26 June 2013 / Published: 2 July 2013| Cited by 1 | PDF Full-text (321 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(3), 436-445; doi:10.3390/pathogens2030436
Received: 2 May 2013; in revised form: 11 June 2013 / Accepted: 18 June 2013 / Published: 26 June 2013| PDF Full-text (351 KB) | HTML Full-text | XML Full-text
Pathogens 2013, 2(1), 92-104; doi:10.3390/pathogens2010092
Received: 9 January 2013; in revised form: 7 February 2013 / Accepted: 9 February 2013 / Published: 18 February 2013| PDF Full-text (1728 KB)
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.
Title: The Role of Extracellular Vesicles in the Transmission and Spread of Prion Infectivity
Authors: Bradley M. Coleman, Belinda Guo and Andrew F. Hill *
Affiliation: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, AUSTRALIA; E-Mail: firstname.lastname@example.org (A.F.H.)
Abstract: Prion diseases are a group of fatal, incurable, transmissible neurodegenerative disorders affecting both humans and animals. Our understanding of prion disease biology has advanced considerably since the discovery that a principal mechanism of these diseases involves the misfolding the host encoded cellular prion protein, PrPC, into the disease associated isoform, PrPSc. Yet, it still remains to be understood as to the cause of neurodegeneration, the molecular structure of the infectious prion, what role other molecules play in disease progression, and how prion infectivity spreads. Here, we discuss our current understanding of prion disease biology and these outstanding questions including recent advances in deciphering the role of extracellular vesicles in the intercellular spread of prions. Extracellular vesicles, such as exosomes and microvesicles are small, membrane bound particles released from a variety of cell types, and have diverse roles in cancer, immunology and the spread of infectious diseases. Growing evidence indicates exosomes play a significant role in the spread of prion disease, as well as other neurodegenerative diseases.
Last update: 6 February 2013