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Animals
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Prion Diseases in Animals
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Prion Diseases in Animals

A special issue of Animals (ISSN 2076-2615). This special issue belongs to the section "Veterinary Clinical Studies".

Deadline for manuscript submissions: 20 June 2025 | Viewed by 2104

Special Issue Editor

Dr. Yong-Chan Kim

E-Mail Website
Guest Editor
Department of Biological Sciences, Andong National University, Andong 36729, Republic of Korea
Interests: neurodegenerative diseases; prion disease

Special Issue Information

Dear Colleagues,

Prion diseases, which include Creutzfeldt–Jakob disease in humans, scrapie in sheep and goats, bovine spongiform encephalopathy in cattle, and chronic wasting disease in elk and deer, are caused by the accumulation of abnormal infectious protein particles in the brain. Conformational conversion of the normal prion protein (PrPC) into the protease K-resistant isoform (PrPSc) is commonly observed in various host animals. Although several studies have investigated many aspects of prion diseases, the diseases are still incurable. Therefore, further studies for the elucidation of the pathogenic mechanisms of the diseases and development of therapeutic interventions against prion diseases are still crucial. This Special Issue welcomes prion researchers who wish to share new findings in animal prion diseases. Original research and review articles about diagnosis, genetic study, pathomechanism, possible biomarkers and potential therapeutic approaches to animal prion diseases are especially welcomed. Studies on nonmammalian prions are also welcome.

Dr. Yong-Chan Kim
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. Animals is an international peer-reviewed open access semimonthly 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 2400 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
  • scrapie
  • BSE
  • CWD
  • TME
  • PrPSc
  • PRNP

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Published Papers (2 papers)

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Research

16 pages, 9111 KiB  
Article
Identification of the Highly Polymorphic Prion Protein Gene (PRNP) in Frogs (Rana dybowskii)
by Chang-Su Han, Sae-Young Won, Sang-Hun Park and Yong-Chan Kim
Animals 2025, 15(2), 220; https://doi.org/10.3390/ani15020220 - 15 Jan 2025
Viewed by 957
Abstract
Prion diseases are fatal neurodegenerative diseases that can be transmitted by infectious protein particles, PrPScs, encoded by the endogenous prion protein gene (PRNP). The origin of prion seeds is unclear, especially in non-human hosts, and this identification is pivotal [...] Read more.
Prion diseases are fatal neurodegenerative diseases that can be transmitted by infectious protein particles, PrPScs, encoded by the endogenous prion protein gene (PRNP). The origin of prion seeds is unclear, especially in non-human hosts, and this identification is pivotal to preventing the spread of prion diseases from host animals. Recently, an abnormally high amyloid propensity in prion proteins (PrPs) was found in a frog, of which the genetic variations in the PRNP gene have not been investigated. In this study, genetic polymorphisms in the PRNP gene were investigated in 194 Dybowski’s frogs using polymerase chain reaction (PCR) and amplicon sequencing. We carried out in silico analyses to predict functional alterations according to non-synonymous single nucleotide polymorphisms (SNPs) using PolyPhen-2, PANTHER, SIFT, and MutPred2. We used ClustalW2 and MEGA X to compare frog PRNP and PrP sequences with those of prion-related animals. To evaluate the impact of the SNPs on protein aggregation propensity and 3D structure, we utilized AMYCO and ColabFold. We identified 34 novel genetic polymorphisms including 6 non-synonymous SNPs in the frog PRNP gene. The hydrogen bond length varied at codons 143 and 207 according to non-synonymous SNPs, even if the electrostatic potential was not changed. In silico analysis predicted S143N to increase the aggregation propensity, and W6L, C8Y, R211W, and L241F had damaging effects on frog PrPs. The PRNP and PrP sequences of frogs showed low homology with those of prion-related mammals. To the best of our knowledge, this study was the first to discover genetic polymorphisms in the PRNP gene in amphibians. Full article
(This article belongs to the Special Issue Prion Diseases in Animals)
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12 pages, 483 KiB  
Article
Impact of Removing the Monitoring Requirements for Holdings with Atypical Scrapie in Great Britain
by Mark Arnold, Bryony Jones, Verity Horigan, Robin Simons and Brenda Rajanayagam
Animals 2024, 14(24), 3607; https://doi.org/10.3390/ani14243607 - 14 Dec 2024
Viewed by 733
Abstract
Atypical scrapie (AS) is a transmissible spongiform encephalopathy (TSE) that affects sheep and goats. Low within-flock incidence suggests that AS is not transmissible between animals, and testing of all animals that exit positive flocks for two years following detection (i.e., intensified monitoring) used [...] Read more.
Atypical scrapie (AS) is a transmissible spongiform encephalopathy (TSE) that affects sheep and goats. Low within-flock incidence suggests that AS is not transmissible between animals, and testing of all animals that exit positive flocks for two years following detection (i.e., intensified monitoring) used to be carried out in the EU to provide data to test this. This intensified monitoring stopped in 2021 but continues in Great Britain (GB). The aim of this study was to predict the number of AS cases missed if this monitoring were also stopped in GB, using a combination of statistical and transmission modelling. The number of AS cases estimated to be missed if the intensified monitoring was stopped was low relative to the number of AS cases detected in other active surveillance streams (e.g., fallen stock and abattoir surveys), at approximately 1 case every 3 years (0.34 per year, 95% CI: 0.18–0.54) compared to 10 per year (95% CI: 4–17) in the active surveillance stream. This suggests that stopping the intensive monitoring of AS would have relatively little impact on AS surveillance and on the power of the available AS data to infer whether AS is contagious. Full article
(This article belongs to the Special Issue Prion Diseases in Animals)
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