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Prions and Prion Diseases 3.0
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Prions and Prion Diseases 3.0

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: closed (30 April 2023) | Viewed by 10005

Special Issue Editor

Prof. Dr. Suehiro Sakaguchi

E-Mail Website
Guest Editor
Division of Molecular Neurobiology, The Institute for Enzyme Research (KOSOKEN), Tokushima University, Tokushima 770-8503, Japan
Interests: prions; neurodegenerative disorders; amyloid; neuronal cell death; protein aggregation
Special Issues, Collections and Topics 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. Dr. Suehiro Sakaguchi
Guest Editor

Manuscript Submission Information

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. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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 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 (5 papers)

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Research

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9 pages, 486 KiB  
Communication
Improved Real-Time Quaking Induced Conversion for Early Diagnostics of Creutzfeldt–Jakob Disease in Denmark
by Remarh Bsoul, Eva Løbner Lund, Kimberley Burns, Mary Andrews, Neil McKenzie, Alison Green and Aušrinė Areškevičiūtė
Int. J. Mol. Sci. 2023, 24(7), 6098; https://doi.org/10.3390/ijms24076098 - 23 Mar 2023
Viewed by 1410
Abstract
Cerebrospinal fluid-based real-time quaking-induced conversion (CSF RT-QuIC) is currently the most prominent method for early detection of sporadic Creutzfeldt–Jakob disease (sCJD), the most common prion disease. CSF RT-QuIC delivers high sensitivity (>90%) and specificity (100%), which has been demonstrated by large ring-trial studies [...] Read more.
Cerebrospinal fluid-based real-time quaking-induced conversion (CSF RT-QuIC) is currently the most prominent method for early detection of sporadic Creutzfeldt–Jakob disease (sCJD), the most common prion disease. CSF RT-QuIC delivers high sensitivity (>90%) and specificity (100%), which has been demonstrated by large ring-trial studies testing probable and definitive sCJD cohorts. Following the inclusion of CSF RT-QuIC in the revised European CJD Surveillance Network diagnostic criteria for sCJD, it has become a standard diagnostic procedure in many prion disease reference or surveillance centers around the world. In this study, we present the implementation of the second-generation CSF RT-QuIC (commonly known as Improved QuIC or IQ) at the Danish Reference Center for Prion Diseases (DRCPD). The method’s sensitivity and specificity were evaluated and validated by analyzing 63 CSF samples. These 63 samples were also analyzed at the National CJD Research and Surveillance Unit (NCJDRSU), based at the University of Edinburgh, UK; analysis was carried out using the first generation or previous CSF RT-QuIC method (PQ). The sensitivity and specificity of PQ during tests at the NCJDRSU were 92% and 100%, respectively. Using these 63 CSF samples, the agreement between the two RT-QuIC generations at DRCPD and NCJDRSU prion laboratories was 100%. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 3.0)
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16 pages, 3019 KiB  
Article
The Effect of Curcuma phaeocaulis Valeton (Zingiberaceae) Extract on Prion Propagation in Cell-Based and Animal Models
by Sungeun Lee, Hakmin Lee, Jaehyeon Kim, Ji Hoon Kim, Eun Mei Gao, Yoonjeong Lee, Miryeong Yoo, Trang H. T. Trinh, Jieun Kim, Chul Young Kim and Chongsuk Ryou
Int. J. Mol. Sci. 2023, 24(1), 182; https://doi.org/10.3390/ijms24010182 - 22 Dec 2022
Cited by 1 | Viewed by 1755
Abstract
Prion diseases are neurodegenerative disorders in humans and animals for which no therapies are currently available. Here, we report that Curcuma phaeocaulis Valeton (Zingiberaceae) (CpV) extract was partly effective in decreasing prion aggregation and propagation in both in vitro and in [...] Read more.
Prion diseases are neurodegenerative disorders in humans and animals for which no therapies are currently available. Here, we report that Curcuma phaeocaulis Valeton (Zingiberaceae) (CpV) extract was partly effective in decreasing prion aggregation and propagation in both in vitro and in vivo models. CpV extract inhibited self-aggregation of recombinant prion protein (PrP) in a test tube assay and decreased the accumulation of scrapie PrP (PrPSc) in ScN2a cells, a cultured neuroblastoma cell line with chronic prion infection, in a concentration-dependent manner. CpV extract also modified the course of the disease in mice inoculated with mouse-adapted scrapie prions, completely preventing the onset of prion disease in three of eight mice. Biochemical and neuropathological analyses revealed a statistically significant reduction in PrPSc accumulation, spongiosis, astrogliosis, and microglia activation in the brains of mice that avoided disease onset. Furthermore, PrPSc accumulation in the spleen of mice was also reduced. CpV extract precluded prion infection in cultured cells as demonstrated by the modified standard scrapie cell assay. This study suggests that CpV extract could contribute to investigating the modulation of prion propagation. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 3.0)
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18 pages, 5124 KiB  
Article
Strain Typing of Classical Scrapie and Bovine Spongiform Encephalopathy (BSE) by Using Ovine PrP (ARQ/ARQ) Overexpressing Transgenic Mice
by Olanrewaju I. Fatola, Markus Keller, Anne Balkema-Buschmann, James Olopade, Martin H. Groschup and Christine Fast
Int. J. Mol. Sci. 2022, 23(12), 6744; https://doi.org/10.3390/ijms23126744 - 16 Jun 2022
Cited by 2 | Viewed by 1771
Abstract
Transmissible spongiform encephalopathies (TSE), caused by abnormal prion protein (PrPSc), affect many species. The most classical scrapie isolates harbor mixtures of strains in different proportions. While the characterization of isolates has evolved from using wild-type mice to transgenic mice, no standardization [...] Read more.
Transmissible spongiform encephalopathies (TSE), caused by abnormal prion protein (PrPSc), affect many species. The most classical scrapie isolates harbor mixtures of strains in different proportions. While the characterization of isolates has evolved from using wild-type mice to transgenic mice, no standardization is established yet. Here, we investigated the incubation period, lesion profile and PrPSc profile induced by well-defined sheep scrapie isolates, bovine spongiform encephalopathy (BSE) and ovine BSE after intracerebral inoculation into two lines of ovine PrP (both ARQ/ARQ) overexpressing transgenic mice (Tgshp IX and Tgshp XI). All isolates were transmitted to both mouse models with an attack rate of almost 100%, but genotype-dependent differences became obvious between the ARQ and VRQ isolates. Surprisingly, BSE induced a much longer incubation period in Tgshp XI compared to Tgshp IX. In contrast to the histopathological lesion profiles, the immunohistochemical PrPSc profiles revealed discriminating patterns in certain brain regions in both models with clear differentiation of both BSE isolates from scrapie. These data provide the basis for the use of Tgshp IX and XI mice in the characterization of TSE isolates. Furthermore, the results enable a deeper appreciation of TSE strain diversity using ovine PrP overexpressing transgenic mice as a biological prion strain typing approach. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 3.0)
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Review

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36 pages, 3444 KiB  
Review
Conventional and State-of-the-Art Detection Methods of Bovine Spongiform Encephalopathy (BSE)
by Monika Olech
Int. J. Mol. Sci. 2023, 24(8), 7135; https://doi.org/10.3390/ijms24087135 - 12 Apr 2023
Cited by 2 | Viewed by 2540
Abstract
Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative disease that belongs to a group of diseases known as transmissible spongiform encephalopathies (TSEs). It is believed that the infectious agent responsible for prion diseases is abnormally folded prion protein (PrPSc), which derives [...] Read more.
Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative disease that belongs to a group of diseases known as transmissible spongiform encephalopathies (TSEs). It is believed that the infectious agent responsible for prion diseases is abnormally folded prion protein (PrPSc), which derives from a normal cellular protein (PrPC), which is a cell surface glycoprotein predominantly expressed in neurons. There are three different types of BSE, the classical BSE (C-type) strain and two atypical strains (H-type and L-type). BSE is primarily a disease of cattle; however, sheep and goats also can be infected with BSE strains and develop a disease clinically and pathogenically indistinguishable from scrapie. Therefore, TSE cases in cattle and small ruminants require discriminatory testing to determine whether the TSE is BSE or scrapie and to discriminate classical BSE from the atypical H- or L-type strains. Many methods have been developed for the detection of BSE and have been reported in numerous studies. Detection of BSE is mainly based on the identification of characteristic lesions or detection of the PrPSc in the brain, often by use of their partial proteinase K resistance properties. The objective of this paper was to summarize the currently available methods, highlight their diagnostic performance, and emphasize the advantages and drawbacks of the application of individual tests. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 3.0)
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15 pages, 1553 KiB  
Review
Systematic Review of Clinical and Pathophysiological Features of Genetic Creutzfeldt–Jakob Disease Caused by a Val-to-Ile Mutation at Codon 180 in the Prion Protein Gene
by Taiki Matsubayashi and Nobuo Sanjo
Int. J. Mol. Sci. 2022, 23(23), 15172; https://doi.org/10.3390/ijms232315172 - 2 Dec 2022
Cited by 2 | Viewed by 1788
Abstract
Genetic Creutzfeldt–Jakob disease (gCJD) is a subtype of genetic prion diseases (gPrDs) caused by the accumulation of mutated pathological prion proteins (PrPSc). gCJD has a phenotypic similarity with sporadic CJD (sCJD). In Japan, gCJD with a Val to Ile substitution at [...] Read more.
Genetic Creutzfeldt–Jakob disease (gCJD) is a subtype of genetic prion diseases (gPrDs) caused by the accumulation of mutated pathological prion proteins (PrPSc). gCJD has a phenotypic similarity with sporadic CJD (sCJD). In Japan, gCJD with a Val to Ile substitution at codon 180 (V180I-gCJD) is the most frequent gPrD, while the mutation is extremely rare in countries other than Japan and Korea. In this article, we aim to review previously elucidated clinical and biochemical features of V180I-gCJD, expecting to advance the understanding of this unique subtype in gCJD. Compared to classical sCJD, specific clinical features of V180I-gCJD include older age at onset, a relatively slow progression of dementia, and a lower positivity for developing myoclonus, cerebellar, pyramidal signs, and visual disturbance. Diffuse edematous ribboning hyperintensity of the cerebral cortex, without occipital lobes in diffusion-weighted magnetic resonance imaging, is also specific. Laboratory data reveal the low positivity of PrPSc in the cerebrospinal fluid and periodic sharp wave complexes on an electroencephalogram. Most patients with V180I-gCJD have been reported to have no family history, probably due to the older age at onset, and clinical and biochemical features indicate the specific phenotype associated with the prion protein gene mutation. Full article
(This article belongs to the Special Issue Prions and Prion Diseases 3.0)
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