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Bordetella Adenylate Cyclase-Hemolysin Toxins
Adenylate cyclase-hemolysin toxin is secreted and produced by three classical species of the genus Bordetella: Bordetella pertussis, B. parapertussis and B. bronchiseptica. This toxin has several properties such as: (i) adenylate cyclase activity, enhanced after interaction with the eukaryotic prote...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618210/ https://www.ncbi.nlm.nih.gov/pubmed/28892012 http://dx.doi.org/10.3390/toxins9090277 |
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author | Guiso, Nicole |
author_facet | Guiso, Nicole |
author_sort | Guiso, Nicole |
collection | PubMed |
description | Adenylate cyclase-hemolysin toxin is secreted and produced by three classical species of the genus Bordetella: Bordetella pertussis, B. parapertussis and B. bronchiseptica. This toxin has several properties such as: (i) adenylate cyclase activity, enhanced after interaction with the eukaryotic protein, calmodulin; (ii) a pore-forming activity; (iii) an invasive activity. It plays an important role in the pathogenesis of these Bordetella species responsible for whooping cough in humans or persistent respiratory infections in mammals, by modulating host immune responses. In contrast with other Bordetella toxins or adhesins, lack of (or very low polymorphism) is observed in the structural gene encoding this toxin, supporting its importance as well as a potential role as a vaccine antigen against whooping cough. In this article, an overview of the investigations undertaken on this toxin is presented. |
format | Online Article Text |
id | pubmed-5618210 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-56182102017-09-29 Bordetella Adenylate Cyclase-Hemolysin Toxins Guiso, Nicole Toxins (Basel) Review Adenylate cyclase-hemolysin toxin is secreted and produced by three classical species of the genus Bordetella: Bordetella pertussis, B. parapertussis and B. bronchiseptica. This toxin has several properties such as: (i) adenylate cyclase activity, enhanced after interaction with the eukaryotic protein, calmodulin; (ii) a pore-forming activity; (iii) an invasive activity. It plays an important role in the pathogenesis of these Bordetella species responsible for whooping cough in humans or persistent respiratory infections in mammals, by modulating host immune responses. In contrast with other Bordetella toxins or adhesins, lack of (or very low polymorphism) is observed in the structural gene encoding this toxin, supporting its importance as well as a potential role as a vaccine antigen against whooping cough. In this article, an overview of the investigations undertaken on this toxin is presented. MDPI 2017-09-11 /pmc/articles/PMC5618210/ /pubmed/28892012 http://dx.doi.org/10.3390/toxins9090277 Text en © 2017 by the author. 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 Guiso, Nicole Bordetella Adenylate Cyclase-Hemolysin Toxins |
title | Bordetella Adenylate Cyclase-Hemolysin Toxins |
title_full | Bordetella Adenylate Cyclase-Hemolysin Toxins |
title_fullStr | Bordetella Adenylate Cyclase-Hemolysin Toxins |
title_full_unstemmed | Bordetella Adenylate Cyclase-Hemolysin Toxins |
title_short | Bordetella Adenylate Cyclase-Hemolysin Toxins |
title_sort | bordetella adenylate cyclase-hemolysin toxins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618210/ https://www.ncbi.nlm.nih.gov/pubmed/28892012 http://dx.doi.org/10.3390/toxins9090277 |
work_keys_str_mv | AT guisonicole bordetellaadenylatecyclasehemolysintoxins |