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Special Issue "Prions and Prion Diseases 2.0"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".

Deadline for manuscript submissions: 30 September 2021.

Special Issue Editor

Prof. Suehiro Sakaguchi
E-Mail Website
Guest Editor
Division of Molecular Neurobiology, Institute for Enzyme Research (KOSOKEN), Tokushima University, Tokushima, Japan
Interests: prions; neurodegenerative disorders; amyloid; neuronal cell death; protein aggregation
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

Prion diseases, which include Creutzfeldt–Jakob disease in humans and scrapie and bovine spongiform encephalopathy in animals, are caused by accumulation of proteinaceous infectious particles, or the so-called prions, in the brain. Conformational conversion of the normal cellular isoform of prion protein, designated PrPC, into the relatively protease-resistant, amyloidogenic isoform, PrPSc, is the underlying mechanism of prion propagation and subsequent degenerative neuronal cell death. Although extensive studies have uncovered many aspects of prion diseases, the diseases still remain incurable. Therefore, further studies for elucidation of the molecular pathogenic mechanisms of the diseases and development of therapeutic interventions against prion diseases are still crucial.

This Special Issue calls for original articles, reviews, and perspectives in relevant research fields, including those for the normal function of PrPC, the neurotoxic mechanism of PrPSc, structural studies of PrPSc, the conversion mechanism of PrPC into PrPSc, elucidation of the molecular mechanism of hereditary prion diseases in humans and animal models, and interventional approaches against prion diseases. Studies on nonmammalian prions are also welcome.

Prof. Suehiro Sakaguchi
Guest Editor

Manuscript Submission Information

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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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • Prion
  • Prion protein
  • Amyloid
  • Neurodegeneration
  • Protein conformation
  • Creutzfeldt–Jakob disease
  • Scrapie
  • Bovine spongiform encephalopathy

Published Papers (2 papers)

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Open AccessArticle
Vaporized Hydrogen Peroxide and Ozone Gas Synergistically Reduce Prion Infectivity on Stainless Steel Wire
Int. J. Mol. Sci. 2021, 22(6), 3268; https://doi.org/10.3390/ijms22063268 - 23 Mar 2021
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Abstract
Prions are infectious agents causing prion diseases, which include Creutzfeldt–Jakob disease (CJD) in humans. Several cases have been reported to be transmitted through medical instruments that were used for preclinical CJD patients, raising public health concerns on iatrogenic transmissions of the disease. Since [...] Read more.
Prions are infectious agents causing prion diseases, which include Creutzfeldt–Jakob disease (CJD) in humans. Several cases have been reported to be transmitted through medical instruments that were used for preclinical CJD patients, raising public health concerns on iatrogenic transmissions of the disease. Since preclinical CJD patients are currently difficult to identify, medical instruments need to be adequately sterilized so as not to transmit the disease. In this study, we investigated the sterilizing activity of two oxidizing agents, ozone gas and vaporized hydrogen peroxide, against prions fixed on stainless steel wires using a mouse bioassay. Mice intracerebrally implanted with prion-contaminated stainless steel wires treated with ozone gas or vaporized hydrogen peroxide developed prion disease later than those implanted with control prion-contaminated stainless steel wires, indicating that ozone gas and vaporized hydrogen peroxide could reduce prion infectivity on wires. Incubation times were further elongated in mice implanted with prion-contaminated stainless steel wires treated with ozone gas-mixed vaporized hydrogen peroxide, indicating that ozone gas mixed with vaporized hydrogen peroxide reduces prions on these wires more potently than ozone gas or vaporized hydrogen peroxide. These results suggest that ozone gas mixed with vaporized hydrogen peroxide might be more useful for prion sterilization than ozone gas or vaporized hydrogen peroxide alone. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 2.0)
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Review

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Open AccessReview
How an Infection of Sheep Revealed Prion Mechanisms in Alzheimer’s Disease and Other Neurodegenerative Disorders
Int. J. Mol. Sci. 2021, 22(9), 4861; https://doi.org/10.3390/ijms22094861 - 04 May 2021
Viewed by 231
Abstract
Although it is not yet universally accepted that all neurodegenerative diseases (NDs) are prion disorders, there is little disagreement that Alzheimer’s disease (AD), Parkinson’s disease, frontotemporal dementia (FTD), and other NDs are a consequence of protein misfolding, aggregation, and spread. This widely accepted [...] Read more.
Although it is not yet universally accepted that all neurodegenerative diseases (NDs) are prion disorders, there is little disagreement that Alzheimer’s disease (AD), Parkinson’s disease, frontotemporal dementia (FTD), and other NDs are a consequence of protein misfolding, aggregation, and spread. This widely accepted perspective arose from the prion hypothesis, which resulted from investigations on scrapie, a common transmissible disease of sheep and goats. The prion hypothesis argued that the causative infectious agent of scrapie was a novel proteinaceous pathogen devoid of functional nucleic acids and distinct from viruses, viroids, and bacteria. At the time, it seemed impossible that an infectious agent like the one causing scrapie could replicate and exist as diverse microbiological strains without nucleic acids. However, aggregates of a misfolded host-encoded protein, designated the prion protein (PrP), were shown to be the cause of scrapie as well as Creutzfeldt–Jakob disease (CJD) and Gerstmann–Sträussler–Scheinker syndrome (GSS), which are similar NDs in humans. This review discusses historical research on diseases caused by PrP misfolding, emphasizing principles of pathogenesis that were later found to be core features of other NDs. For example, the discovery that familial prion diseases can be caused by mutations in PrP was important for understanding prion replication and disease susceptibility not only for rare PrP diseases but also for far more common NDs involving other proteins. We compare diseases caused by misfolding and aggregation of APP-derived Aβ peptides, tau, and α-synuclein with PrP prion disorders and argue for the classification of NDs caused by misfolding of these proteins as prion diseases. Deciphering the molecular pathogenesis of NDs as prion-mediated has provided new approaches for finding therapies for these intractable, invariably fatal disorders and has revolutionized the field. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 2.0)
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