Cargando…
Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue
Staphylococcus aureus secretes a number of host-injurious toxins, among the most prominent of which is the small β-barrel pore-forming toxin α-hemolysin. Initially named based on its properties as a red blood cell lytic toxin, early studies suggested a far greater complexity of α-hemolysin action as...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3717774/ https://www.ncbi.nlm.nih.gov/pubmed/23888516 http://dx.doi.org/10.3390/toxins5061140 |
_version_ | 1782277726982373376 |
---|---|
author | Berube, Bryan J. Bubeck Wardenburg, Juliane |
author_facet | Berube, Bryan J. Bubeck Wardenburg, Juliane |
author_sort | Berube, Bryan J. |
collection | PubMed |
description | Staphylococcus aureus secretes a number of host-injurious toxins, among the most prominent of which is the small β-barrel pore-forming toxin α-hemolysin. Initially named based on its properties as a red blood cell lytic toxin, early studies suggested a far greater complexity of α-hemolysin action as nucleated cells also exhibited distinct responses to intoxication. The hemolysin, most aptly referred to as α-toxin based on its broad range of cellular specificity, has long been recognized as an important cause of injury in the context of both skin necrosis and lethal infection. The recent identification of ADAM10 as a cellular receptor for α-toxin has provided keen insight on the biology of toxin action during disease pathogenesis, demonstrating the molecular mechanisms by which the toxin causes tissue barrier disruption at host interfaces lined by epithelial or endothelial cells. This review highlights both the historical studies that laid the groundwork for nearly a century of research on α-toxin and key findings on the structural and functional biology of the toxin, in addition to discussing emerging observations that have significantly expanded our understanding of this toxin in S. aureus disease. The identification of ADAM10 as a proteinaceous receptor for the toxin not only provides a greater appreciation of truths uncovered by many historic studies, but now affords the opportunity to more extensively probe and understand the role of α-toxin in modulation of the complex interaction of S. aureus with its human host. |
format | Online Article Text |
id | pubmed-3717774 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-37177742013-07-22 Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue Berube, Bryan J. Bubeck Wardenburg, Juliane Toxins (Basel) Review Staphylococcus aureus secretes a number of host-injurious toxins, among the most prominent of which is the small β-barrel pore-forming toxin α-hemolysin. Initially named based on its properties as a red blood cell lytic toxin, early studies suggested a far greater complexity of α-hemolysin action as nucleated cells also exhibited distinct responses to intoxication. The hemolysin, most aptly referred to as α-toxin based on its broad range of cellular specificity, has long been recognized as an important cause of injury in the context of both skin necrosis and lethal infection. The recent identification of ADAM10 as a cellular receptor for α-toxin has provided keen insight on the biology of toxin action during disease pathogenesis, demonstrating the molecular mechanisms by which the toxin causes tissue barrier disruption at host interfaces lined by epithelial or endothelial cells. This review highlights both the historical studies that laid the groundwork for nearly a century of research on α-toxin and key findings on the structural and functional biology of the toxin, in addition to discussing emerging observations that have significantly expanded our understanding of this toxin in S. aureus disease. The identification of ADAM10 as a proteinaceous receptor for the toxin not only provides a greater appreciation of truths uncovered by many historic studies, but now affords the opportunity to more extensively probe and understand the role of α-toxin in modulation of the complex interaction of S. aureus with its human host. MDPI 2013-06-13 /pmc/articles/PMC3717774/ /pubmed/23888516 http://dx.doi.org/10.3390/toxins5061140 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Berube, Bryan J. Bubeck Wardenburg, Juliane Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue |
title | Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue |
title_full | Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue |
title_fullStr | Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue |
title_full_unstemmed | Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue |
title_short | Staphylococcus aureus α-Toxin: Nearly a Century of Intrigue |
title_sort | staphylococcus aureus α-toxin: nearly a century of intrigue |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3717774/ https://www.ncbi.nlm.nih.gov/pubmed/23888516 http://dx.doi.org/10.3390/toxins5061140 |
work_keys_str_mv | AT berubebryanj staphylococcusaureusatoxinnearlyacenturyofintrigue AT bubeckwardenburgjuliane staphylococcusaureusatoxinnearlyacenturyofintrigue |