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Molecular Genetics of Prion Diseases
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Molecular Genetics of Prion Diseases

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 (31 December 2020) | Viewed by 35462

Special Issue Editor

Dr. Byung-Hoon Jeong

E-Mail Website
Guest Editor
Korea Zoonosis Research Institute, Jeonbuk National University, Iksan 54531, Jeonbuk, Republic of Korea
Interests: prion diseases; neurodegenerative disorders; prion protein gene (PRNP); prion-like protein gene (PRND); shadow of prion protein gene (SPRN); prion-related protein gene (PRNT); genetics; genomics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Prion disease is fatal, acute and irreversible neurodegenerative diseases with wide host ranges, including scrapie in sheep and goats, bovine spongiform encephalopathy (BSE) in cattle, chronic wasting disease (CWD) in elk and deer, and Creutzfeldt–Jakob disease (CJD) in humans. It has been approximately three centuries since prion disease in sheep was first discovered in 1732. However, the exact mechanism on the progression and the causative agent of prion diseases have not been revealed thus far. To date, genetic variations including genetic polymorphisms, germline mutations and somatic mutations of the prion disease-related genes play pivotal role in prion diseases.

In this Special Issue of the International Journal of Molecular Sciences, the main topic will be “Molecular genetics of prion diseases”, which is dedicated to research articles and reviews of prion disease-related genetic studies, including human and non-human studies. The emphasis will be on novel prion disease-related genetic variabilities and prion disease susceptibilities and the functional role of prion disease-related genes to understand the pathogenesis of prion diseases.

Dr. Byung-Hoon Jeong
Guest Editor

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Keywords

  • Prion diseases
  • Prion protein gene (PRNP)
  • Prion-like protein gene (PRND)
  • Shadow of prion protein gene (SPRN)
  • Prion-related protein gene (PRNT)
  • Prion disease-candidate genes
  • Genetics
  • Genomics
  • Bioinformatics

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Published Papers (6 papers)

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Research

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18 pages, 11174 KiB  
Article
Regional Differences in Neuroinflammation-Associated Gene Expression in the Brain of Sporadic Creutzfeldt–Jakob Disease Patients
by Aušrinė Areškevičiūtė, Thomas Litman, Helle Broholm, Linea C. Melchior, Pia R. Nielsen, Alison Green, Jens O. Eriksen, Colin Smith and Eva L. Lund
Int. J. Mol. Sci. 2021, 22(1), 140; https://doi.org/10.3390/ijms22010140 - 25 Dec 2020
Cited by 9 | Viewed by 3865
Abstract
Neuroinflammation is an essential part of neurodegeneration. Yet, the current understanding of neuroinflammation-associated molecular events in distinct brain regions of prion disease patients is insufficient to lay the ground for effective treatment strategies targeting this complex neuropathological process. To address this problem, we [...] Read more.
Neuroinflammation is an essential part of neurodegeneration. Yet, the current understanding of neuroinflammation-associated molecular events in distinct brain regions of prion disease patients is insufficient to lay the ground for effective treatment strategies targeting this complex neuropathological process. To address this problem, we analyzed the expression of 800 neuroinflammation-associated genes to create a profile of biological processes taking place in the frontal cortex and cerebellum of patients who suffered from sporadic Creutzfeldt–Jakob disease. The analysis was performed using NanoString nCounter technology with human neuroinflammation panel+. The observed gene expression patterns were regionally and sub-regionally distinct, suggesting a variable neuroinflammatory response. Interestingly, the observed differences could not be explained by the molecular subtypes of sporadic Creutzfeldt–Jakob disease. Furthermore, analyses of canonical pathways and upstream regulators based on differentially expressed genes indicated an overlap between biological processes taking place in different brain regions. This suggests that even smaller-scale spatial data reflecting subtle changes in brain cells’ functional heterogeneity and their immediate pathologic microenvironments are needed to explain the observed differential gene expression in a greater detail. Full article
(This article belongs to the Special Issue Molecular Genetics of Prion Diseases)
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11 pages, 965 KiB  
Article
First Report of the Potential Bovine Spongiform Encephalopathy (BSE)-Related Somatic Mutation E211K of the Prion Protein Gene (PRNP) in Cattle
by Sae-Young Won, Yong-Chan Kim and Byung-Hoon Jeong
Int. J. Mol. Sci. 2020, 21(12), 4246; https://doi.org/10.3390/ijms21124246 - 15 Jun 2020
Cited by 19 | Viewed by 4050
Abstract
Bovine spongiform encephalopathy (BSE) is a prion disease characterized by spongiform degeneration and astrocytosis in the brain. Unlike classical BSE, which is caused by prion-disease-contaminated meat and bone meal, the cause of atypical BSE has not been determined. Since previous studies have reported [...] Read more.
Bovine spongiform encephalopathy (BSE) is a prion disease characterized by spongiform degeneration and astrocytosis in the brain. Unlike classical BSE, which is caused by prion-disease-contaminated meat and bone meal, the cause of atypical BSE has not been determined. Since previous studies have reported that the somatic mutation in the human prion protein gene (PRNP) has been linked to human prion disease, the somatic mutation of the PRNP gene was presumed to be one cause of prion disease. However, to the best of our knowledge, the somatic mutation of this gene in cattle has not been investigated to date. We investigated somatic mutations in a total of 58 samples, including peripheral blood; brain tissue including the medulla oblongata, cerebellum, cortex, and thalamus; and skin tissue in 20 individuals from each breed using pyrosequencing. In addition, we estimated the deleterious effect of the K211 somatic mutation on bovine prion protein by in silico evaluation tools, including PolyPhen-2 and PANTHER. We found a high rate of K211 somatic mutations of the bovine PRNP gene in the medulla oblongata of three Holsteins (10% ± 4.4%, 28% ± 2%, and 19.55% ± 3.1%). In addition, in silico programs showed that the K211 somatic mutation was damaging. To the best of our knowledge, this study is the first to investigate K211 somatic mutations of the bovine PRNP gene that are associated with potential BSE progression. Full article
(This article belongs to the Special Issue Molecular Genetics of Prion Diseases)
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16 pages, 4600 KiB  
Article
Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene (PRNP) in Dogs—A Resistant Animal of Prion Disease
by Dong-Ju Kim, Yong-Chan Kim, An-Dang Kim and Byung-Hoon Jeong
Int. J. Mol. Sci. 2020, 21(11), 4160; https://doi.org/10.3390/ijms21114160 - 10 Jun 2020
Cited by 17 | Viewed by 3449
Abstract
Transmissible spongiform encephalopathies (TSEs) have been reported in a wide range of species. However, TSE infection in natural cases has never been reported in dogs. Previous studies have reported that polymorphisms of the prion protein gene (PRNP) have a direct impact [...] Read more.
Transmissible spongiform encephalopathies (TSEs) have been reported in a wide range of species. However, TSE infection in natural cases has never been reported in dogs. Previous studies have reported that polymorphisms of the prion protein gene (PRNP) have a direct impact on the susceptibility of TSE. However, studies on polymorphisms of the canine PRNP gene are very rare in dogs. We examined the genotype, allele, and haplotype frequencies of canine PRNP in 204 dogs using direct sequencing and analyzed linkage disequilibrium (LD) using Haploview version 4.2. In addition, to evaluate the impact of nonsynonymous polymorphisms on the function of prion protein (PrP), we carried out in silico analysis using PolyPhen-2, PROVEAN, and PANTHER. Furthermore, we analyzed the structure of PrP and hydrogen bonds according to alleles of nonsynonymous single nucleotide polymorphisms (SNPs) using the Swiss-Pdb Viewer program. Finally, we predicted the impact of the polymorphisms on the aggregation propensity of dog PrP using AMYCO. We identified a total of eight polymorphisms, including five novel SNPs and one insertion/deletion polymorphism, and found strong LDs and six major haplotypes among eight polymorphisms. In addition, we identified significantly different distribution of haplotypes among eight dog breeds, however, the kinds of identified polymorphisms were different among each dog breed. We predicted that p.64_71del HGGGWGQP, Asp182Gly, and Asp182Glu polymorphisms can impact the function and/or structure of dog PrP. Furthermore, the number of hydrogen bonds of dog PrP with the Glu182 and Gly182 alleles were predicted to be less than those with the Asp182 allele. Finally, Asp163Glu and Asp182Gly showed more aggregation propensity than wild-type dog PrP. These results suggest that nonsynonymous SNPs, Asp182Glu and Asp182Gly, can influence the stability of dog PrP and confer the possibility of TSE infection in dogs. Full article
(This article belongs to the Special Issue Molecular Genetics of Prion Diseases)
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Review

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24 pages, 5082 KiB  
Review
Cervid Prion Protein Polymorphisms: Role in Chronic Wasting Disease Pathogenesis
by Maria Immaculata Arifin, Samia Hannaoui, Sheng Chun Chang, Simrika Thapa, Hermann M. Schatzl and Sabine Gilch
Int. J. Mol. Sci. 2021, 22(5), 2271; https://doi.org/10.3390/ijms22052271 - 25 Feb 2021
Cited by 38 | Viewed by 6238
Abstract
Chronic wasting disease (CWD) is a prion disease found in both free-ranging and farmed cervids. Susceptibility of these animals to CWD is governed by various exogenous and endogenous factors. Past studies have demonstrated that polymorphisms within the prion protein (PrP) sequence itself affect [...] Read more.
Chronic wasting disease (CWD) is a prion disease found in both free-ranging and farmed cervids. Susceptibility of these animals to CWD is governed by various exogenous and endogenous factors. Past studies have demonstrated that polymorphisms within the prion protein (PrP) sequence itself affect an animal’s susceptibility to CWD. PrP polymorphisms can modulate CWD pathogenesis in two ways: the ability of the endogenous prion protein (PrPC) to convert into infectious prions (PrPSc) or it can give rise to novel prion strains. In vivo studies in susceptible cervids, complemented by studies in transgenic mice expressing the corresponding cervid PrP sequence, show that each polymorphism has distinct effects on both PrPC and PrPSc. It is not entirely clear how these polymorphisms are responsible for these effects, but in vitro studies suggest they play a role in modifying PrP epitopes crucial for PrPC to PrPSc conversion and determining PrPC stability. PrP polymorphisms are unique to one or two cervid species and most confer a certain degree of reduced susceptibility to CWD. However, to date, there are no reports of polymorphic cervid PrP alleles providing absolute resistance to CWD. Studies on polymorphisms have focused on those found in CWD-endemic areas, with the hope that understanding the role of an animal’s genetics in CWD can help to predict, contain, or prevent transmission of CWD. Full article
(This article belongs to the Special Issue Molecular Genetics of Prion Diseases)
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18 pages, 1062 KiB  
Review
Neuroinflammation in Prion Disease
by Bei Li, Meiling Chen and Caihong Zhu
Int. J. Mol. Sci. 2021, 22(4), 2196; https://doi.org/10.3390/ijms22042196 - 23 Feb 2021
Cited by 27 | Viewed by 12829
Abstract
Neuroinflammation, typically manifest as microglial activation and astrogliosis accompanied by transcriptomic alterations, represents a common hallmark of various neurodegenerative conditions including prion diseases. Microglia play an overall neuroprotective role in prion disease, whereas reactive astrocytes with aberrant phenotypes propagate prions and contribute to [...] Read more.
Neuroinflammation, typically manifest as microglial activation and astrogliosis accompanied by transcriptomic alterations, represents a common hallmark of various neurodegenerative conditions including prion diseases. Microglia play an overall neuroprotective role in prion disease, whereas reactive astrocytes with aberrant phenotypes propagate prions and contribute to prion-induced neurodegeneration. The existence of heterogeneous subpopulations and dual functions of microglia and astrocytes in prion disease make them potential targets for therapeutic intervention. A variety of neuroinflammation-related molecules are involved in prion pathogenesis. Therapeutics targeting neuroinflammation represents a novel approach to combat prion disease. Deciphering neuroinflammation in prion disease will deepen our understanding of pathogenesis of other neurodegenerative disorders. Full article
(This article belongs to the Special Issue Molecular Genetics of Prion Diseases)
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15 pages, 1715 KiB  
Review
Neurometals in the Pathogenesis of Prion Diseases
by Masahiro Kawahara, Midori Kato-Negishi and Ken-ichiro Tanaka
Int. J. Mol. Sci. 2021, 22(3), 1267; https://doi.org/10.3390/ijms22031267 - 28 Jan 2021
Cited by 19 | Viewed by 3939
Abstract
Prion diseases are progressive and transmissive neurodegenerative diseases. The conformational conversion of normal cellular prion protein (PrPC) into abnormal pathogenic prion protein (PrPSc) is critical for its infection and pathogenesis. PrPC possesses the ability to bind to various [...] Read more.
Prion diseases are progressive and transmissive neurodegenerative diseases. The conformational conversion of normal cellular prion protein (PrPC) into abnormal pathogenic prion protein (PrPSc) is critical for its infection and pathogenesis. PrPC possesses the ability to bind to various neurometals, including copper, zinc, iron, and manganese. Moreover, increasing evidence suggests that PrPC plays essential roles in the maintenance of homeostasis of these neurometals in the synapse. In addition, trace metals are critical determinants of the conformational change and toxicity of PrPC. Here, we review our studies and other new findings that inform the current understanding of the links between trace elements and physiological functions of PrPC and the neurotoxicity of PrPSc. Full article
(This article belongs to the Special Issue Molecular Genetics of Prion Diseases)
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