Latest Research on Prion Diseases

A special issue of Pathogens (ISSN 2076-0817). This special issue belongs to the section "Prions".

Deadline for manuscript submissions: closed (20 May 2022) | Viewed by 6981

Special Issue Editors

Department of Psychiatry, Wroclaw Medical University, 50-367 Wroclaw, Poland
Interests: Alzheimer’s disease; cognitive Impairment; neurodegeneration; neurogenerative disease
Tokyo Metropolitan Industrial Technology Research Institute, Japan
Interests: prion; prion disease; neurodegeneration; mitochondria; protein chaperone

Special Issue Information

Dear Colleagues,

The term “prion” was coined to describe a family of proteinaceous infectious particles that include pathogens as well as viruses and bacteria, with the disease caused by them being named prion disease. Although we have been aware of the existence of prions for almost 40 years already, the physiological function of the prion protein, which is the main body of the pathogen, is still not well understood. Therefore, scientifically uncertain aspects cannot be completely wiped out, and this means that prion disease remains fatal. As such, it is crucial to understand the prion protein, which forms the basis of the prion concept from a scientific viewpoint, and to develop a therapeutic method for prion disease.

In this special issue, we will accept a wide range of manuscripts (including research articles and reviews) from the viewpoint of basic cell biology, and the fields of medicine and veterinary medicine, including bovine spongiform encephalopathy (BSE), to understand prion as a pathogen.

We look forward to your valuable contributions in this Special Edition that will facilitate further development in this exciting field.

Prof. Jerzy Leszek
Prof. Naomi Hachiya
Guest Editors

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. 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 2700 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

  • prion
  • prion protein
  • prion diseases
  • development of treatment for prion disease
  • zoonotic disease
  • bovine spongiform encephalopathy (BSE)

Published Papers (2 papers)

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Research

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13 pages, 3009 KiB  
Article
Detection of Prions in Brain Homogenates and CSF Samples Using a Second-Generation RT-QuIC Assay: A Useful Tool for Retrospective Analysis of Archived Samples
by Tibor Moško, Soňa Galušková, Radoslav Matěj, Magdalena Brůžová and Karel Holada
Pathogens 2021, 10(6), 750; https://0-doi-org.brum.beds.ac.uk/10.3390/pathogens10060750 - 13 Jun 2021
Cited by 8 | Viewed by 2152
Abstract
The possibilities for diagnosing prion diseases have shifted significantly over the last 10 years. The RT-QuIC assay option has been added for neuropsychiatric symptoms, supporting biomarkers and final post-mortem confirmation. Samples of brain homogenates used for final diagnosis, archived for many years, provide [...] Read more.
The possibilities for diagnosing prion diseases have shifted significantly over the last 10 years. The RT-QuIC assay option has been added for neuropsychiatric symptoms, supporting biomarkers and final post-mortem confirmation. Samples of brain homogenates used for final diagnosis, archived for many years, provide the possibility for retrospective studies. We used a second-generation RT-QuIC assay to detect seeding activity in different types of sporadic and genetic prion diseases in archival brain homogenates and post-mortem CSF samples that were 2 to 15 years old. Together, we tested 92 archival brain homogenates: 39 with definite prion disease, 28 with definite other neurological disease, and 25 with no signs of neurological disorders. The sensitivity and specificity of the assay were 97.4% and 100%, respectively. Differences were observed in gCJD E200K, compared to the sporadic CJD group. In 52 post-mortem CSF samples—24 with definite prion disease and 28 controls—we detected the inhibition of seeding reaction due to high protein content. Diluting the samples eliminated such inhibition and led to 95.8% sensitivity and 100% specificity of the assay. In conclusion, we proved the reliability of archived brain homogenates and post-mortem CSF samples for retrospective analysis by RT-QuIC after long-term storage, without changed reactivity. Full article
(This article belongs to the Special Issue Latest Research on Prion Diseases)
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Review

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11 pages, 270 KiB  
Review
The Latest Research on RT-QuIC Assays—A Literature Review
by Thi-Thu-Trang Dong and Katsuya Satoh
Pathogens 2021, 10(3), 305; https://0-doi-org.brum.beds.ac.uk/10.3390/pathogens10030305 - 05 Mar 2021
Cited by 14 | Viewed by 3534
Abstract
The misfolding of proteins such as the prion protein, α-synuclein, and tau represents a key initiating event for pathogenesis of most common neurodegenerative disorders, and its presence correlates with infectivity. To date, the diagnosis of these disorders mainly relied on the recognition of [...] Read more.
The misfolding of proteins such as the prion protein, α-synuclein, and tau represents a key initiating event for pathogenesis of most common neurodegenerative disorders, and its presence correlates with infectivity. To date, the diagnosis of these disorders mainly relied on the recognition of clinical symptoms when neurodegeneration was already at an advanced phase. In recent years, several efforts have been made to develop new diagnostic tools for the early diagnosis of prion diseases. The real-time quaking-induced conversion (RT–QuIC) assay, an in vitro assay that can indirectly detect very low amounts of PrPSc aggregates, has provided a very promising tool to improve the early diagnosis of human prion diseases. Over the decade since RT–QuIC was introduced, the diagnosis of not only prion diseases but also synucleinopathies and tauopathies has greatly improved. Therefore, in our study, we summarize the current trends and knowledge of RT–QuIC assays, as well as discuss the diagnosis of neurodegenerative diseases using RT–QuIC assays, which have been updated in recent years. Full article
(This article belongs to the Special Issue Latest Research on Prion Diseases)
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