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Viruses
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Prion Neuroinvasion
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Prion Neuroinvasion

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Prions".

Deadline for manuscript submissions: closed (15 October 2021) | Viewed by 14623

Special Issue Editors

Dr. Anthony E. Kincaid

E-Mail
Guest Editor
Department of Pharmacy Sciences, School of Pharmacy and Health Professions, Creighton University, Omaha, NE, USA
Interests: prion pathogenesis;specifically the characterization of routes of entry and mechanisms of centripetal and centrifugal spread of prions in the nervous system
Special Issues, Collections and Topics in MDPI journals
Dr. Jason C. Bartz

E-Mail Website
Guest Editor
Department of Medical Microbiology and Immunology, School of Medicine, Creighton University, Omaha, NE 68178, USA
Interests: Prions; Prion disease

Special Issue Information

Dear Colleagues,

Prion diseases are a class of fatal neurodegenerative diseases that affect animals, including humans. The causative agent is a misfolded protein that is sometimes inherited and sometimes the result of an iatrogenic procedure, but more commonly, prions gain access to the interior of the body by crossing the epithelium of the gut, nasal cavity, or the skin.

While much work has been done on the pathogenesis of prion diseases, there are several questions that remain unanswered, including the cellular and molecular events of prions crossing the epithelial tissue, the role of blood in the spread of prions, the specific mechanism(s) of how prions enter and spread centripetally in the peripheral and central nervous systems, and how prions spread centrifugally to peripheral tissues where they are shed.

The focus of this Special Issue is the process of prion entry and neuroinvasion, the spread of prions in the central and peripheral nervous systems, and the mechanism(s) of neuronal cell death.

Dr. Anthony E. Kincaid
Dr. Jason C. Bartz
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. Viruses 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 2600 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 pathogenesis
  • prion entry
  • prion neuroinvasion
  • transport in nerves
  • spread in the central nervous system
  • centrifugal and centripetal spread of prions
  • prionemia

Published Papers (5 papers)

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Research

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11 pages, 1155 KiB  
Article
Detection of Chronic Wasting Disease Prions in Fetal Tissues of Free-Ranging White-Tailed Deer
by Amy V. Nalls, Erin E. McNulty, Amber Mayfield, James M. Crum, Michael K. Keel, Edward A. Hoover, Mark G. Ruder and Candace K. Mathiason
Viruses 2021, 13(12), 2430; https://0-doi-org.brum.beds.ac.uk/10.3390/v13122430 - 03 Dec 2021
Cited by 12 | Viewed by 2359
Abstract
The transmission of chronic wasting disease (CWD) has largely been attributed to contact with infectious prions shed in excretions (saliva, urine, feces, blood) by direct animal-to-animal exposure or indirect contact with the environment. Less-well studied has been the role that mother-to-offspring transmission may [...] Read more.
The transmission of chronic wasting disease (CWD) has largely been attributed to contact with infectious prions shed in excretions (saliva, urine, feces, blood) by direct animal-to-animal exposure or indirect contact with the environment. Less-well studied has been the role that mother-to-offspring transmission may play in the facile transmission of CWD, and whether mother-to-offspring transmission before birth may contribute to the extensive spread of CWD. We thereby focused on a population of free-ranging white-tailed deer from West Virginia, USA, in which CWD has been detected. Fetal tissues, ranging from 113 to 158 days of gestation, were harvested from the uteri of CWD+ dams in the asymptomatic phase of infection. Using serial protein misfolding amplification (sPMCA), we detected evidence of prion seeds in 7 of 14 fetuses (50%) from 7 of 9 pregnancies (78%), with the earliest detection at 113 gestational days. This is the first report of CWD detection in free ranging white-tailed deer fetal tissues. Further investigation within cervid populations across North America will help define the role and impact of mother-to-offspring vertical transmission of CWD. Full article
(This article belongs to the Special Issue Prion Neuroinvasion)
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14 pages, 12707 KiB  
Article
Deletion of Kif5c Does Not Alter Prion Disease Tempo or Spread in Mouse Brain
by Brent Race, Katie Williams, Chase Baune, James F. Striebel, Clayton W. Winkler, James A. Carroll, Sandra E. Encalada and Bruce Chesebro
Viruses 2021, 13(7), 1391; https://0-doi-org.brum.beds.ac.uk/10.3390/v13071391 - 17 Jul 2021
Viewed by 2641
Abstract
In prion diseases, the spread of infectious prions (PrPSc) is thought to occur within nerves and across synapses of the central nervous system (CNS). However, the mechanisms by which PrPSc moves within axons and across nerve synapses remain undetermined. Molecular motors, including kinesins [...] Read more.
In prion diseases, the spread of infectious prions (PrPSc) is thought to occur within nerves and across synapses of the central nervous system (CNS). However, the mechanisms by which PrPSc moves within axons and across nerve synapses remain undetermined. Molecular motors, including kinesins and dyneins, transport many types of intracellular cargo. Kinesin-1C (KIF5C) has been shown to transport vesicles carrying the normal prion protein (PrPC) within axons, but whether KIF5C is involved in PrPSc axonal transport is unknown. The current study tested whether stereotactic inoculation in the striatum of KIF5C knock-out mice (Kif5c−/−) with 0.5 µL volumes of mouse-adapted scrapie strains 22 L or ME7 would result in an altered rate of prion spreading and/or disease timing. Groups of mice injected with each strain were euthanized at either pre-clinical time points or following the development of prion disease. Immunohistochemistry for PrP was performed on brain sections and PrPSc distribution and tempo of spread were compared between mouse strains. In these experiments, no differences in PrPSc spread, distribution or survival times were observed between C57BL/6 and Kif5c−/− mice. Full article
(This article belongs to the Special Issue Prion Neuroinvasion)
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Review

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31 pages, 3290 KiB  
Review
Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases
by Zoe J. Lambert, Justin J. Greenlee, Eric D. Cassmann and M. Heather West Greenlee
Viruses 2021, 13(12), 2453; https://0-doi-org.brum.beds.ac.uk/10.3390/v13122453 - 07 Dec 2021
Cited by 5 | Viewed by 3138
Abstract
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death. TSEs occur when the endogenous cellular prion protein (PrPC) misfolds to form the pathological prion protein (PrPSc), which [...] Read more.
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death. TSEs occur when the endogenous cellular prion protein (PrPC) misfolds to form the pathological prion protein (PrPSc), which templates further conversion of PrPC to PrPSc, accumulates, and initiates a cascade of pathologic processes in cells and tissues. Different strains of prion disease within a species are thought to arise from the differential misfolding of the prion protein and have different clinical phenotypes. Different strains of prion disease may also result in differential accumulation of PrPSc in brain regions and tissues of natural hosts. Here, we review differential accumulation that occurs in the retinal ganglion cells, cerebellar cortex and white matter, and plexuses of the enteric nervous system in cattle with bovine spongiform encephalopathy, sheep and goats with scrapie, cervids with chronic wasting disease, and humans with prion diseases. By characterizing TSEs in their natural host, we can better understand the pathogenesis of different prion strains. This information is valuable in the pursuit of evaluating and discovering potential biomarkers and therapeutics for prion diseases. Full article
(This article belongs to the Special Issue Prion Neuroinvasion)
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14 pages, 2284 KiB  
Review
The Role of the Nasal Cavity in the Pathogenesis of Prion Diseases
by Anthony E. Kincaid
Viruses 2021, 13(11), 2287; https://0-doi-org.brum.beds.ac.uk/10.3390/v13112287 - 16 Nov 2021
Cited by 1 | Viewed by 2480
Abstract
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a class of fatal neurodegenerative diseases caused by the entry and spread of infectious prion proteins (PrPSc) in the central nervous system (CNS). These diseases are endemic to certain mammalian animal species that [...] Read more.
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a class of fatal neurodegenerative diseases caused by the entry and spread of infectious prion proteins (PrPSc) in the central nervous system (CNS). These diseases are endemic to certain mammalian animal species that use their sense of smell for a variety of purposes and therefore expose their nasal cavity (NC) to PrPSc in the environment. Prion diseases that affect humans are either inherited due to a mutation of the gene that encodes the prion protein, acquired by exposure to contaminated tissues or medical devices, or develop without a known cause (referred to as sporadic). The purpose of this review is to identify components of the NC that are involved in prion transport and to summarize the evidence that the NC serves as a route of entry (centripetal spread) and/or a source of shedding (centrifugal spread) of PrPSc, and thus plays a role in the pathogenesis of the TSEs. Full article
(This article belongs to the Special Issue Prion Neuroinvasion)
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17 pages, 1276 KiB  
Review
The Neural Gut–Brain Axis of Pathological Protein Aggregation in Parkinson’s Disease and Its Counterpart in Peroral Prion Infections
by Michael Beekes
Viruses 2021, 13(7), 1394; https://0-doi-org.brum.beds.ac.uk/10.3390/v13071394 - 18 Jul 2021
Cited by 4 | Viewed by 3100
Abstract
A neuropathological hallmark of Parkinson’s disease (PD) is the cerebral deposition of abnormally aggregated α-synuclein (αSyn). PD-associated αSyn (αSynPD) aggregates are assumed to act, in a prion-like manner, as proteinaceous nuclei (“seeds”) capable of self-templated propagation. Braak and colleagues put forward [...] Read more.
A neuropathological hallmark of Parkinson’s disease (PD) is the cerebral deposition of abnormally aggregated α-synuclein (αSyn). PD-associated αSyn (αSynPD) aggregates are assumed to act, in a prion-like manner, as proteinaceous nuclei (“seeds”) capable of self-templated propagation. Braak and colleagues put forward the idea of a neural gut-brain axis mediating the centripetal spread of αSynPD pathology from the enteric nervous system (ENS) to the brain in PD. This has sparked great interest and initiated passionate discussions both in support of and opposing the suggested hypothesis. A precedent for the spread of protein seeds or seeding from the gastro-intestinal (GI) tract to the central nervous system (CNS) had been previously revealed for pathological prion protein in peroral prion infections. This article scrutinizes the similarities and dissimilarities between the pathophysiological spread of disease-associated protein aggregation along the neural gut–brain axis in peroral prion infections and PD. On this basis, evidence supporting the proposed neural gut–brain axis in PD is concluded to be not as robust as that established for peroral prion infections. New tools for the ultrasensitive detection of αSynPD-associated seeding activity in archived or fresh human tissue samples such as real-time quaking induced conversion (RT-QuIC) or protein misfolding cyclic amplification (PMCA) assays can possibly help to address this deficit in the future. Full article
(This article belongs to the Special Issue Prion Neuroinvasion)
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