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Biomolecules
Special Issues
New Insights into Prion and Prion-Like Diseases
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New Insights into Prion and Prion-Like Diseases

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (15 March 2023) | Viewed by 6841

Special Issue Editors

Dr. Iryna Benilova

E-Mail Website
Guest Editor
MRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, London, UK
Interests: prions; prion-like diseases; amyloid; aggregation; neurodegeneration
Dr. Amaia M. Arranz

E-Mail Website
Guest Editor
Achucarro Basque Center for Neuroscience, Science Park of the UPV/EHU, Leioa, Spain
Interests: induced pluripotent stem cells (iPSCs); humanized models; neuroinflammation; amyloid; neurodegeneration; Alzheimer’s disease

Special Issue Information

Dear Colleagues,

Prion diseases are rare sporadic, acquired, or inherited proteinopathies that cause fatal neurodegeneration in humans and animals and share key features with other more common degenerative brain diseases associated with protein aggregation. Ongoing multiplication of disease-associated protein aggregates triggers microglia and astrocyte activation, calcium dyshomeostasis and organellar stress ending up in synaptic network abnormalities and dementia symptoms.

Recent advances in deciphering the molecular structure of infectious prions, amyloid-beta and tau aggregates from diseased brain implicate a link between a specific structure of a misfolded protein and a certain neuropathological phenotype; however, the precise cellular processes that lead to neuronal loss of function and death remain a black box impinging on therapeutic development. Availability of improved humanized models of prion-like diseases will be critical for the translational success of preclinical studies in this challenging field.

The goal of this Special Issue of Biomolecules is to publish recent research comprising original studies as well as reviews that will advance our understanding of prion and prion-like diseases by providing mechanistic insight into:

  • structure–function relationships between the disease-associated aggregates (prions, amyloid-beta, tau, alpha-synuclein, TDP-43, and others) and specific pathological phenotypes triggered in cellular, ex vivo, and in vivo models

  • prion-like mechanisms in non-prion neurodegenerative proteinopathies such as Alzheimer’s disease and others

  • cellular signaling cascades elicited or impaired by pathological aggregation, propagation and spread of prions and prion-like proteins with a focus of potential drug targets

Dr. Iryna Benilova
Dr. Amaia M. Arranz
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. Biomolecules 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

  • prions
  • prion-like proteins
  • neurodegeneration
  • synaptic dysfunction
  • aggregation
  • propagation
  • structure–function relationship

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Published Papers (3 papers)

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Research

14 pages, 10390 KiB  
Article
Strain-Dependent Morphology of Reactive Astrocytes in Human- and Animal-Vole-Adapted Prions
by Rosalia Bruno, Geraldina Riccardi, Floriana Iacobone, Flavia Chiarotti, Laura Pirisinu, Ilaria Vanni, Stefano Marcon, Claudia D’Agostino, Matteo Giovannelli, Piero Parchi, Umberto Agrimi, Romolo Nonno and Michele Angelo Di Bari
Biomolecules 2023, 13(5), 757; https://doi.org/10.3390/biom13050757 - 27 Apr 2023
Cited by 1 | Viewed by 1776
Abstract
Reactive astrogliosis is one of the pathological hallmarks of prion diseases. Recent studies highlighted the influence of several factors on the astrocyte phenotype in prion diseases, including the brain region involved, the genotype backgrounds of the host, and the prion strain. Elucidating the [...] Read more.
Reactive astrogliosis is one of the pathological hallmarks of prion diseases. Recent studies highlighted the influence of several factors on the astrocyte phenotype in prion diseases, including the brain region involved, the genotype backgrounds of the host, and the prion strain. Elucidating the influence of prion strains on the astrocyte phenotype may provide crucial insights for developing therapeutic strategies. Here, we investigated the relationship between prion strains and astrocyte phenotype in six human- and animal-vole-adapted strains characterized by distinctive neuropathological features. In particular, we compared astrocyte morphology and astrocyte-associated PrPSc deposition among strains in the same brain region, the mediodorsal thalamic nucleus (MDTN). Astrogliosis was detected to some extent in the MDTN of all analyzed voles. However, we observed variability in the morphological appearance of astrocytes depending on the strain. Astrocytes displayed variability in thickness and length of cellular processes and cellular body size, suggesting strain-specific phenotypes of reactive astrocytes. Remarkably, four out of six strains displayed astrocyte-associated PrPSc deposition, which correlated with the size of astrocytes. Overall, these data show that the heterogeneous reactivity of astrocytes in prion diseases depends at least in part on the infecting prion strains and their specific interaction with astrocytes. Full article
(This article belongs to the Special Issue New Insights into Prion and Prion-Like Diseases)
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10 pages, 10631 KiB  
Article
Gerstmann–Sträussler–Scheinker Disease with F198S Mutation Induces Independent Tau and Prion Protein Pathologies in Bank Voles
by Rosalia Bruno, Laura Pirisinu, Geraldina Riccardi, Claudia D’Agostino, Elena De Cecco, Giuseppe Legname, Franco Cardone, Pierluigi Gambetti, Romolo Nonno, Umberto Agrimi and Michele Angelo Di Bari
Biomolecules 2022, 12(10), 1537; https://doi.org/10.3390/biom12101537 - 21 Oct 2022
Cited by 1 | Viewed by 1986
Abstract
Gerstmann–Sträussler–Scheinker disease (GSS) is a rare genetic prion disease. A large GSS kindred linked to the serine-for-phenylalanine substitution at codon 198 of the prion protein gene (GSS-F198S) is characterized by conspicuous accumulation of prion protein (PrP)-amyloid deposits and neurofibrillary tangles. Recently, we demonstrated [...] Read more.
Gerstmann–Sträussler–Scheinker disease (GSS) is a rare genetic prion disease. A large GSS kindred linked to the serine-for-phenylalanine substitution at codon 198 of the prion protein gene (GSS-F198S) is characterized by conspicuous accumulation of prion protein (PrP)-amyloid deposits and neurofibrillary tangles. Recently, we demonstrated the transmissibility of GSS-F198S prions to bank vole carrying isoleucine at 109 PrP codon (BvI). Here we investigated: (i) the transmissibility of GSS-F198S prions to voles carrying methionine at codon 109 (BvM); (ii) the induction of hyperphosphorylated Tau (pTau) in two vole lines, and (iii) compared the phenotype of GSS-F198S-induced pTau with pTau induced in BvM following intracerebral inoculation of a familial Alzheimer’s disease case carrying Presenilin 1 mutation (fAD-PS1). We did not detect prion transmission to BvM, despite the high susceptibility of BvI previously observed. Immunohistochemistry established the presence of induced pTau depositions in vole brains that were not affected by prions. Furthermore, the phenotype of pTau deposits in vole brains was similar in GSS-F198S and fAD-PS1. Overall, results suggest that, regardless of the cause of pTau deposition and its relationship with PrPSc in GSS-F198S human-affected brains, the two components possess their own seeding properties, and that pTau deposition is similarly induced by GSS-F198S and fAD-PS1. Full article
(This article belongs to the Special Issue New Insights into Prion and Prion-Like Diseases)
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16 pages, 2850 KiB  
Article
Modeling the Competition between Misfolded Aβ Conformers That Produce Distinct Types of Amyloid Pathology in Alzheimer’s Disease
by Guilian Xu, Susan Fromholt and David R. Borchelt
Biomolecules 2022, 12(7), 886; https://doi.org/10.3390/biom12070886 - 24 Jun 2022
Cited by 2 | Viewed by 2086
Abstract
The amyloid pathology characteristic of Alzheimer’s disease (AD) can be broadly classified as either fibrillary amyloid or diffuse amyloid. Fibrillary amyloid is found in cored-neuritic deposits, fibrillar deposits, and vascular deposits, and binds strongly to the amyloid revealing dyes Thioflavin-S or Congo Red. [...] Read more.
The amyloid pathology characteristic of Alzheimer’s disease (AD) can be broadly classified as either fibrillary amyloid or diffuse amyloid. Fibrillary amyloid is found in cored-neuritic deposits, fibrillar deposits, and vascular deposits, and binds strongly to the amyloid revealing dyes Thioflavin-S or Congo Red. Diffuse amyloid can appear as wispy dispersed deposits or compact tufted deposits dispersed in neuropil, and binds amyloid dyes weakly if at all. In AD brains, both types of pathology are detected. Homogenates from AD brains, or the brains of transgenic mice modeling AD-amyloidosis, have been used to seed pathology in vulnerable host transgenic models. These studies suggest that pathologies may arise from distinct conformers or strains of misfolded Aβ, similar to propagating prions. Using Aβ strains sourced from four different AD-amyloidosis models, we injected pathological seeds into the brains of newborn mice from three different transgenic hosts with distinctive Aβ pathologies. Two of the seeding sources were from mice that primarily develop cored-neuritic Aβ deposits (cored strain) while the other two seeding sources were from mice that develop diffuse Aβ deposits (diffuse strain). These seeds were injected into host APP mice in which the resident strain was either diffuse or cored-neuritic pathology. Seeding-homogenates were injected into the brains of newborn mice to initiate propagation as early as possible. Depending upon the level of transgene expression in the host, we show that the injected strains of misfolded Aβ from the seeding homogenate were able to outcompete the resident strain of the APP host model. In serial passaging experiments, it appeared that the diffuse strain was more easily propagated than the cored strain. Collectively, our studies align with the idea that different types of Aβ pathology in AD brains arise from different populations of Aβ conformers that compete to populate the brain. Full article
(This article belongs to the Special Issue New Insights into Prion and Prion-Like Diseases)
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