Special Issue "Prions and Prion-like Transmissible Protein Pathogens"

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

Deadline for manuscript submissions: closed (31 May 2020).

Special Issue Editors

Dr. Wenquan Zou

Guest Editor
Departments of Pathology and Neurology, Case Western Reserve University School of Medicine, Adelbert Road, Room 403, Cleveland, OH 44106, USA
Prof. Jiyan Ma
Website
Co-Guest Editor
Center for Neurodegenerative Science, Van Andel Research Institute,333 Bostwick Avenue N.E, Grand Rapids, MI 49503, USA
Interests: Parkinson’s disease, prion disease, protein aggregation in neurodegenerative diseases, prions, pathogenesis of neurodegenerative

Special Issue Information

Dear Colleagues,

Prions are infectious proteins that are associated with a group of transmissible neurodegenerative diseases in humans and animals, such as Creutzfeldt–Jakob disease in humans, scrapie in sheep and goats, mad cow disease in cattle, and chronic wasting disease in elk and deer. Unlike traditional pathogens such as bacteria and viruses that always require genetic material DNA for their propagation, the infectious prion proteins are able to propagate and duplicate and spread from individual to individual in the absence of DNA. Interestingly, prion-like proteins have also recently been observed in other neurodegenerative diseases, such as Alzheimer disease, Parkinson’s disease, amyotrophic lateral sclerosis, etc. These share the prion-like features of propagation and transmission from cell to cell, although in contrast to prions, transmission from individual to individual has not be reported in these prion-like misfolded proteins. Now, prions have become the prototypes for these emerging groups of transmissible protein pathogens.
The annual international Prion conference will take place from May 21–24, 2019 in Edmonton, Alberta, Canada. This Special Issue welcomes prion researchers and experts who wish to highlight new developments in prions and prion-like transmissible misfolded protein pathogens that emerge in the conference. In addition, we shall also accept original research and review articles about pathogenesis, diagnosis, and potential therapeutic responses to human and animal prion diseases. We especially 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.
We look forward to your contributions and to a valuable Special Edition that will promote further developments in this exciting field.

Dr. Wenquan Zou
Prof. Jiyan Ma
Guest Editors

Manuscript Submission Information

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Keywords

  • Prions
  • Prion diseases
  • Prion-like
  • Prion 2019 conference
  • Neurodegenerative disorders
  • Protein misfolding disorders
  • Protein aggregations
  • Neuroscience
  • Alzheimer’s disease
  • Parkinson’s disease
  • Glycosylation

Published Papers (3 papers)

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Research

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Open AccessArticle
Long-Term Incubation PrPCWD with Soils Affects Prion Recovery but Not Infectivity
Pathogens 2020, 9(4), 311; https://doi.org/10.3390/pathogens9040311 - 23 Apr 2020
Abstract
Chronic wasting disease (CWD) is a contagious prion disease of cervids. The infectious agent is shed from animals at the preclinical and clinical stages of disease where it persists in the environment as a reservoir of CWD infectivity. In this study, we demonstrate [...] Read more.
Chronic wasting disease (CWD) is a contagious prion disease of cervids. The infectious agent is shed from animals at the preclinical and clinical stages of disease where it persists in the environment as a reservoir of CWD infectivity. In this study, we demonstrate that long-term incubation of CWD prions (generated from tg-mice infected with deer or elk prions) with illite, montmorillonite (Mte) and whole soils results in decreased recovery of PrPCWD, suggesting that binding becomes more avid and irreversible with time. This continual decline of immunoblot PrPCWD detection did not correlate with prion infectivity levels. Bioassay showed no significant differences in incubation periods between mice inoculated with 1% CWD brain homogenate (BH) and with the CWD-BH pre-incubated with quartz or Luvisolic Ae horizon for 1 or 30 weeks. After 55 weeks incubation with Chernozem and Luvisol, bound PrPCWD was not detectable by immunoblotting but remained infectious. This study shows that although recovery of PrPCWD bound to soil minerals and whole soils with time become more difficult, prion infectivity is not significantly altered. Detection of prions in soil is, therefore, not only affected by soil type but also by length of time of the prion–soil interaction. Full article
(This article belongs to the Special Issue Prions and Prion-like Transmissible Protein Pathogens)
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Open AccessFeature PaperArticle
PrPSc with Seeding Activity Extensively Overlaps with Proteinase-Resistant PrPSc Rather than Infectious PrPSc
Pathogens 2020, 9(3), 241; https://doi.org/10.3390/pathogens9030241 - 24 Mar 2020
Abstract
The disease-associated prion protein (PrPSc) has the ability to seed the conformational conversion of normal prion proteins into the amyloid fibril form. This prion seeding activity can be measured using an in vitro amplification assay termed real-time quaking-induced conversion (RT-QuIC). There is a [...] Read more.
The disease-associated prion protein (PrPSc) has the ability to seed the conformational conversion of normal prion proteins into the amyloid fibril form. This prion seeding activity can be measured using an in vitro amplification assay termed real-time quaking-induced conversion (RT-QuIC). There is a strong correlation between RT-QuIC positivity and prion infection; however, the relationship between seeding activity and infectivity remains elusive. In this study, we used endpoint dilution RT-QuIC on the brain homogenates from wild-type mice with mouse-adopted bovine spongiform encephalopathy (mBSE) at defined intervals during the incubation period and evaluated the temporal relationship among prion seeding dose, levels of proteinase-resistant PrPSc (PrPres), and infectious titer. We found that the infectious titer reached a plateau by 100 days postinfection, whereas seeding dose and PrPres levels were continuously elevated. Our calculation showed that the doubling time (dt) for seeding dose from 40 to 100 days postinoculation was closer to the dt for PrPres levels than to the dt for prion titer. Although an uncoupling of seeding doses and PrPres levels was observed at end-stage disease in this model, our findings suggest that there is substantial but not complete overlap between PrPSc with seeding activity and PrPres rather than infectious PrPSc. Full article
(This article belongs to the Special Issue Prions and Prion-like Transmissible Protein Pathogens)
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Review

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Open AccessReview
Immunotherapy against Prion Disease
by Yue Ma and Jiyan Ma
Pathogens 2020, 9(3), 216; https://doi.org/10.3390/pathogens9030216 - 14 Mar 2020
Abstract
The term “prion disease” encompasses a group of neurodegenerative diseases affecting both humans and animals. Currently, there is no effective therapy and all forms of prion disease are invariably fatal. Because of (a) the outbreak of bovine spongiform encephalopathy in cattle and variant [...] Read more.
The term “prion disease” encompasses a group of neurodegenerative diseases affecting both humans and animals. Currently, there is no effective therapy and all forms of prion disease are invariably fatal. Because of (a) the outbreak of bovine spongiform encephalopathy in cattle and variant Creutzfeldt–Jakob disease in humans; (b) the heated debate about the prion hypothesis; and (c) the availability of a natural prion disease in rodents, the understanding of the pathogenic process in prion disease is much more advanced compared to that of other neurodegenerative disorders, which inspired many attempts to develop therapeutic strategies against these fatal diseases. In this review, we focus on immunotherapy against prion disease. We explain our rationale for immunotherapy as a plausible therapeutic choice, review previous trials using either active or passive immunization, and discuss potential strategies for overcoming the hurdles in developing a successful immunotherapy. We propose that immunotherapy is a plausible and practical therapeutic strategy and advocate more studies in this area to develop effective measures to control and treat these devastating disorders. Full article
(This article belongs to the Special Issue Prions and Prion-like Transmissible Protein Pathogens)
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