Chronic Wasting Disease and Other Animal Prion Diseases: Towards the Comprehension of Animal Prion Pathologies

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

Deadline for manuscript submissions: 31 August 2024 | Viewed by 1846

Special Issue Editors


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Guest Editor
Centro de Encefalopatías y Enfermedades Transmisibles Emergentes, University of Zaragoza, 50013 Zaragoza, Spain
Interests: prion diseases; chronic wasting disease; scrapie; bovine spongiform encephalopathy; PrP; pathology

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Guest Editor
Faculty of Agricultural, Life and Environmental Sciences, Department of Renewable Resources, University of Alberta, Edmonton, AB T6G 2G8, Canada
Interests: chronic wasting disease; animals; prion proteins

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Guest Editor
1. Department of Pathology and Laboratory Medicine, University of Ottawa, Ottawa, ON K1N 6N5, Canada
2. Anatomical Pathology, Department of Pathology and Laboratory Medicine, Institute of Eastern Ontario Regional Laboratory Association, Ottawa Hospital Civic Location, Ottawa, ON K1Y 4E9, Canada
Interests: CNS pathogens; prions; Creutzfeldt-Jakob disease; surveillance

Special Issue Information

Dear Colleagues,

Prion diseases are neurodegenerative, fatal processes of animals and humans caused by prions, which are infectious, aberrant proteins that can propagate in the absence of genetic material. Along with scrapie, the prion disease of sheep and goats, Chronic Wasting Disease (CWD), which affects numerous species of cervids, stands out for being highly transmissible. CWD is unique among prion diseases since it is the only one found in both wild and domestic animals.

Many aspects of prion diseases remain to be elucidated. These include the specific molecular mechanisms involved in their pathogenesis or which molecules could be used as biomarkers for a preclinical diagnosis or treatment. However, one of the most puzzling features about prions is that, like other pathological agents, exist in a variety of strains that produce different disease phenotypes and have different host ranges. Since prions do not contain genetic material, the biological information of prion strains it is believed to be encoded in, and perpetuated by, their conformation.

This Special Issue welcomes prion researchers who wish to share new developments in CWD and other animal prion diseases. Original research and review articles about animal prion strains, pathogenesis, possible biomarkers for diagnosis and potential therapeutic approaches to prion diseases are especially welcomed.

Dr. Alicia Otero
Dr. Alsu Kuznetsova
Dr. Gerard H. Jansen
Guest Editors

Manuscript Submission Information

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Keywords

  • prion diseases
  • animal prions
  • CWD
  • scrapie
  • BSE
  • prion pathogenesis
  • prion strains

Published Papers (2 papers)

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Research

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13 pages, 6625 KiB  
Article
A Comparison of RML Prion Inactivation Efficiency by Heterogeneous and Homogeneous Photocatalysis
by Ioannis Paspaltsis, Eirini Kanata, Sotirios Sotiriadis, Susana Silva Correia, Matthias Schmitz, Inga Zerr, Dimitra Dafou, Konstantinos Xanthopoulos and Theodoros Sklaviadis
Pathogens 2024, 13(5), 420; https://doi.org/10.3390/pathogens13050420 - 16 May 2024
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Abstract
Prions are proteinaceous pathogens responsible for a variety of devastating diseases in mammals, including scrapie in sheep and goats, chronic wasting disease in cervids, and Creutzfeldt–Jakob disease (CJD) in humans. They are characterized by their exceptional persistence to common inactivation procedures. This applies [...] Read more.
Prions are proteinaceous pathogens responsible for a variety of devastating diseases in mammals, including scrapie in sheep and goats, chronic wasting disease in cervids, and Creutzfeldt–Jakob disease (CJD) in humans. They are characterized by their exceptional persistence to common inactivation procedures. This applies to all possible sources of prion contamination as prions may be present in the tissues and biological fluids of infected individuals. Hence, efficient prion inactivation procedures are still being sought to minimize the risk of intra- or inter-species transmission. In the past, photocatalytic treatment has been proven to be capable of efficiently oxidizing and inactivating prions. In the present study, the efficacy of homogeneous photo-Fenton-based photocatalysis as well as heterogeneous photocatalysis with TiO2 in reducing RML mouse scrapie infectivity was evaluated. Prion inactivation was assessed by means of a bioassay, and the results were confirmed by in vitro experiments. While the prion infectivity of the RML mouse scrapie was reduced after treatment with the photo-Fenton reagent, the heterogeneous photocatalytic treatment of the same prion strain completely eliminated prion infectivity. Full article
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15 pages, 355 KiB  
Review
Diagnosis in Scrapie: Conventional Methods and New Biomarkers
by Diego Sola, Marina Betancor, Paula A. Marco Lorente, Sonia Pérez Lázaro, Tomás Barrio, Eloisa Sevilla, Belén Marín, Bernardino Moreno, Marta Monzón, Cristina Acín, Rosa Bolea, Juan J. Badiola and Alicia Otero
Pathogens 2023, 12(12), 1399; https://doi.org/10.3390/pathogens12121399 - 28 Nov 2023
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Abstract
Scrapie, a naturally occurring prion disease affecting goats and sheep, comprises classical and atypical forms, with classical scrapie being the archetype of transmissible spongiform encephalopathies. This review explores the challenges of scrapie diagnosis and the utility of various biomarkers and their potential implications [...] Read more.
Scrapie, a naturally occurring prion disease affecting goats and sheep, comprises classical and atypical forms, with classical scrapie being the archetype of transmissible spongiform encephalopathies. This review explores the challenges of scrapie diagnosis and the utility of various biomarkers and their potential implications for human prion diseases. Understanding these biomarkers in the context of scrapie may enable earlier prion disease diagnosis in humans, which is crucial for effective intervention. Research on scrapie biomarkers bridges the gap between veterinary and human medicine, offering hope for the early detection and improved management of prion diseases. Full article
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