Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i>
Biofilm formation is important for infection by many pathogens. <i>Bordetella bronchiseptica</i> causes respiratory tract infections in mammals and forms biofilm structures in nasal epithelium of infected mice. We previously demonstrated that cyclic di-GMP is involved in biofilm formatio...
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2016
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Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/86497 |
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I19-R120-10915-86497 |
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institution |
Universidad Nacional de La Plata |
institution_str |
I-19 |
repository_str |
R-120 |
collection |
SEDICI (UNLP) |
language |
Inglés |
topic |
Ciencias Exactas Bordetella bronchiseptica respiratory tract infections |
spellingShingle |
Ciencias Exactas Bordetella bronchiseptica respiratory tract infections Ambrosis, Nicolás Martín Boyd, Chelsea D. O'Toole, George A. Fernández, Julieta Sisti, Federico Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i> |
topic_facet |
Ciencias Exactas Bordetella bronchiseptica respiratory tract infections |
description |
Biofilm formation is important for infection by many pathogens. <i>Bordetella bronchiseptica</i> causes respiratory tract infections in mammals and forms biofilm structures in nasal epithelium of infected mice. We previously demonstrated that cyclic di-GMP is involved in biofilm formation in <i>B. bronchiseptica</i>. In the present work, based on their previously reported function in <i>Pseudomonas fluorescens</i>, we identified three genes in the <i>B. bronchiseptica</i> genome likely involved in c-di-GMP-dependent biofilm formation: brtA, lapD and lapG. Genetic analysis confirmed a role for BrtA, LapD and LapG in biofilm formation using microtiter plate assays, as well as scanning electron and fluorescent microscopy to analyze the phenotypes of mutants lacking these proteins. <i>In vitro</i> and <i>in vivo</i> studies showed that the protease LapG of <i>B. bronchiseptica</i> cleaves the N-terminal domain of BrtA, as well as the LapA protein of <i>P. fluorescens</i>, indicating functional conservation between these species. Furthermore, while BrtA and LapG appear to have little or no impact on colonization in a mouse model of infection, a <i>B. bronchiseptica</i> strain lacking the LapG protease has a significantly higher rate of inducing a severe disease outcome compared to the wild type. These findings support a role for c-di-GMP acting through BrtA/LapD/LapG to modulate biofilm formation, as well as impact pathogenesis, by <i>B. bronchiseptica</i>. |
format |
Articulo Articulo |
author |
Ambrosis, Nicolás Martín Boyd, Chelsea D. O'Toole, George A. Fernández, Julieta Sisti, Federico |
author_facet |
Ambrosis, Nicolás Martín Boyd, Chelsea D. O'Toole, George A. Fernández, Julieta Sisti, Federico |
author_sort |
Ambrosis, Nicolás Martín |
title |
Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i> |
title_short |
Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i> |
title_full |
Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i> |
title_fullStr |
Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i> |
title_full_unstemmed |
Homologs of the LapD-LapG c-di-GMP effector system control biofilm formation by <i>Bordetella bronchiseptica</i> |
title_sort |
homologs of the lapd-lapg c-di-gmp effector system control biofilm formation by <i>bordetella bronchiseptica</i> |
publishDate |
2016 |
url |
http://sedici.unlp.edu.ar/handle/10915/86497 |
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bdutipo_str |
Repositorios |
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1764820489738387456 |