Next Article in Journal
Ginsenoside Rg1 Suppresses Type 2 PRRSV Infection via NF-κB Signaling Pathway In Vitro, and Provides Partial Protection against HP-PRRSV in Piglet
Previous Article in Journal
Seasonal Dynamics of Algae-Infecting Viruses and Their Inferred Interactions with Protists
Previous Article in Special Issue
Molecular Piracy: Redirection of Bacteriophage Capsid Assembly by Mobile Genetic Elements
Open AccessReview

Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates

by Byron Caughey 1,* and Allison Kraus 2,*
Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA
Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA
Authors to whom correspondence should be addressed.
Viruses 2019, 11(11), 1044; (registering DOI)
Received: 26 September 2019 / Revised: 5 November 2019 / Accepted: 6 November 2019 / Published: 9 November 2019
(This article belongs to the Special Issue Viruses Ten-Year Anniversary)
The prion-like spreading and accumulation of specific protein aggregates appear to be central to the pathogenesis of many human diseases, including Alzheimer’s and Parkinson’s. Accumulating evidence indicates that inoculation of tissue extracts from diseased individuals into suitable experimental animals can in many cases induce the aggregation of the disease-associated protein, as well as related pathological lesions. These findings, together with the history of the prion field, have raised the questions about whether such disease-associated protein aggregates are transmissible between humans by casual or iatrogenic routes, and, if so, do they propagate enough in the new host to cause disease? These practical considerations are important because real, and perhaps even only imagined, risks of human-to-human transmission of diseases such as Alzheimer’s and Parkinson’s may force costly changes in clinical practice that, in turn, are likely to have unintended consequences. The prion field has taught us that a single protein, PrP, can aggregate into forms that can propagate exponentially in vitro, but range from being innocuous to deadly when injected into experimental animals in ways that depend strongly on factors such as conformational subtleties, routes of inoculation, and host responses. In assessing the hazards posed by various disease-associated, self-propagating protein aggregates, it is imperative to consider both their actual transmissibilities and the pathological consequences of their propagation, if any, in recipient hosts. View Full-Text
Keywords: prion; amyloid; infectivity; pathogenesis; transmission; tau; synuclein; amyloid-β prion; amyloid; infectivity; pathogenesis; transmission; tau; synuclein; amyloid-β
Show Figures

Figure 1

MDPI and ACS Style

Caughey, B.; Kraus, A. Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates. Viruses 2019, 11, 1044.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop