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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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Autor principal: Guiso, Nicole
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
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.
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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
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