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Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates
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 an...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6893620/ https://www.ncbi.nlm.nih.gov/pubmed/31717531 http://dx.doi.org/10.3390/v11111044 |
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author | Caughey, Byron Kraus, Allison |
author_facet | Caughey, Byron Kraus, Allison |
author_sort | Caughey, Byron |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6893620 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-68936202019-12-23 Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates Caughey, Byron Kraus, Allison Viruses Review 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. MDPI 2019-11-09 /pmc/articles/PMC6893620/ /pubmed/31717531 http://dx.doi.org/10.3390/v11111044 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Caughey, Byron Kraus, Allison Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates |
title | Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates |
title_full | Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates |
title_fullStr | Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates |
title_full_unstemmed | Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates |
title_short | Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates |
title_sort | transmissibility versus pathogenicity of self-propagating protein aggregates |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6893620/ https://www.ncbi.nlm.nih.gov/pubmed/31717531 http://dx.doi.org/10.3390/v11111044 |
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