Special Issue "Prion Neuroinvasion"

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

Deadline for manuscript submissions: 15 October 2021.

Special Issue Editors

Dr. Anthony E. Kincaid
E-Mail Website
Guest Editor
Department of Pharmacy Sciences, School of Pharmacy and Health Professions, Creighton Universitydisabled, Omaha, USA
Interests: prion pathogenesis;specifically the characterization of routes of entry and mechanisms of centripetal and centrifugal spread of prions in the nervous system
Dr. Jason C. Bartz
E-Mail Website
Guest Editor
Department of Medical Microbiology and Immunology, School of Medicine, Creighton University, Omaha, Nebraska, USA
Interests: prion strain biology;prion pathogenesis;environmental fate of prions

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

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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 (2 papers)

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Research

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Article
Deletion of Kif5c Does Not Alter Prion Disease Tempo or Spread in Mouse Brain
Viruses 2021, 13(7), 1391; https://doi.org/10.3390/v13071391 - 17 Jul 2021
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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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Review
The Neural Gut–Brain Axis of Pathological Protein Aggregation in Parkinson’s Disease and Its Counterpart in Peroral Prion Infections
Viruses 2021, 13(7), 1394; https://doi.org/10.3390/v13071394 - 18 Jul 2021
Viewed by 589
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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