Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>

Autores
Sisti, Federico; Ha, Dae-Gon; O'Toole, George A.; Hozbor, Daniela Flavia; Fernández, Julieta
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The signalling molecule bis-(39–59)-cyclic-dimeric guanosine monophosphate (c-di-GMP) is a central regulator of diverse cellular functions, including motility, biofilm formation, cell cycle progression and virulence, in bacteria. Multiple diguanylate cyclase and phosphodiesterasedomain-containing proteins (GGDEF and EAL/HD-GYP, respectively) modulate the levels of the second messenger c-di-GMP to transmit signals and obtain such specific cellular responses. In the genus Bordetella this c-di-GMP network is poorly studied. In this work, we evaluated the expression of two phenotypes in Bordetella bronchiseptica regulated by c-di-GMP, biofilm formation and motility, under the influence of ectopic expression of Pseudomonas aeruginosa proteins with EAL or GGDEF domains that regulates the c-di-GMP level. In agreement with previous reports for other bacteria, we observed that B. bronchiseptica is able to form biofilm and reduce its motility only when GGDEF domain protein is expressed. Moreover we identify a GGDEF domain protein (BB3576) with diguanylate cyclase activity that participates in motility and biofilm regulation in B. bronchiseptica. These results demonstrate for the first time, to our knowledge, the presence of c-di-GMP regulatory signalling in B. bronchiseptica.
Instituto de Biotecnologia y Biologia Molecular
Materia
Ciencias Exactas
Bordetella bronchiseptica
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/107998
Acceder
id SEDICI_3a1ac52ab990b64feb6dcf3c71be566c
oai_identifier_str oai:sedici.unlp.edu.ar:10915/107998
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>Sisti, FedericoHa, Dae-GonO'Toole, George A.Hozbor, Daniela FlaviaFernández, JulietaCiencias ExactasBordetella bronchisepticaThe signalling molecule bis-(39–59)-cyclic-dimeric guanosine monophosphate (c-di-GMP) is a central regulator of diverse cellular functions, including motility, biofilm formation, cell cycle progression and virulence, in bacteria. Multiple diguanylate cyclase and phosphodiesterasedomain-containing proteins (GGDEF and EAL/HD-GYP, respectively) modulate the levels of the second messenger c-di-GMP to transmit signals and obtain such specific cellular responses. In the genus Bordetella this c-di-GMP network is poorly studied. In this work, we evaluated the expression of two phenotypes in Bordetella bronchiseptica regulated by c-di-GMP, biofilm formation and motility, under the influence of ectopic expression of Pseudomonas aeruginosa proteins with EAL or GGDEF domains that regulates the c-di-GMP level. In agreement with previous reports for other bacteria, we observed that B. bronchiseptica is able to form biofilm and reduce its motility only when GGDEF domain protein is expressed. Moreover we identify a GGDEF domain protein (BB3576) with diguanylate cyclase activity that participates in motility and biofilm regulation in B. bronchiseptica. These results demonstrate for the first time, to our knowledge, the presence of c-di-GMP regulatory signalling in B. bronchiseptica.Instituto de Biotecnologia y Biologia Molecular2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf869-879http://sedici.unlp.edu.ar/handle/10915/107998enginfo:eu-repo/semantics/altIdentifier/url/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC4085988&blobtype=pdfinfo:eu-repo/semantics/altIdentifier/issn/1465-2080info:eu-repo/semantics/altIdentifier/pmid/23475948info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.064345-0info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:23:56Zoai:sedici.unlp.edu.ar:10915/107998Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:23:56.886SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
title Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
spellingShingle Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
Sisti, Federico
Ciencias Exactas
Bordetella bronchiseptica
title_short Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
title_full Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
title_fullStr Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
title_full_unstemmed Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
title_sort Cyclic-di-GMP signalling regulates motility and biofilm formation in <i>Bordetella bronchiseptica</i>
dc.creator.none.fl_str_mv Sisti, Federico
Ha, Dae-Gon
O'Toole, George A.
Hozbor, Daniela Flavia
Fernández, Julieta
author Sisti, Federico
author_facet Sisti, Federico
Ha, Dae-Gon
O'Toole, George A.
Hozbor, Daniela Flavia
Fernández, Julieta
author_role author
author2 Ha, Dae-Gon
O'Toole, George A.
Hozbor, Daniela Flavia
Fernández, Julieta
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Bordetella bronchiseptica
topic Ciencias Exactas
Bordetella bronchiseptica
dc.description.none.fl_txt_mv The signalling molecule bis-(39–59)-cyclic-dimeric guanosine monophosphate (c-di-GMP) is a central regulator of diverse cellular functions, including motility, biofilm formation, cell cycle progression and virulence, in bacteria. Multiple diguanylate cyclase and phosphodiesterasedomain-containing proteins (GGDEF and EAL/HD-GYP, respectively) modulate the levels of the second messenger c-di-GMP to transmit signals and obtain such specific cellular responses. In the genus Bordetella this c-di-GMP network is poorly studied. In this work, we evaluated the expression of two phenotypes in Bordetella bronchiseptica regulated by c-di-GMP, biofilm formation and motility, under the influence of ectopic expression of Pseudomonas aeruginosa proteins with EAL or GGDEF domains that regulates the c-di-GMP level. In agreement with previous reports for other bacteria, we observed that B. bronchiseptica is able to form biofilm and reduce its motility only when GGDEF domain protein is expressed. Moreover we identify a GGDEF domain protein (BB3576) with diguanylate cyclase activity that participates in motility and biofilm regulation in B. bronchiseptica. These results demonstrate for the first time, to our knowledge, the presence of c-di-GMP regulatory signalling in B. bronchiseptica.
Instituto de Biotecnologia y Biologia Molecular
description The signalling molecule bis-(39–59)-cyclic-dimeric guanosine monophosphate (c-di-GMP) is a central regulator of diverse cellular functions, including motility, biofilm formation, cell cycle progression and virulence, in bacteria. Multiple diguanylate cyclase and phosphodiesterasedomain-containing proteins (GGDEF and EAL/HD-GYP, respectively) modulate the levels of the second messenger c-di-GMP to transmit signals and obtain such specific cellular responses. In the genus Bordetella this c-di-GMP network is poorly studied. In this work, we evaluated the expression of two phenotypes in Bordetella bronchiseptica regulated by c-di-GMP, biofilm formation and motility, under the influence of ectopic expression of Pseudomonas aeruginosa proteins with EAL or GGDEF domains that regulates the c-di-GMP level. In agreement with previous reports for other bacteria, we observed that B. bronchiseptica is able to form biofilm and reduce its motility only when GGDEF domain protein is expressed. Moreover we identify a GGDEF domain protein (BB3576) with diguanylate cyclase activity that participates in motility and biofilm regulation in B. bronchiseptica. These results demonstrate for the first time, to our knowledge, the presence of c-di-GMP regulatory signalling in B. bronchiseptica.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/107998
url http://sedici.unlp.edu.ar/handle/10915/107998
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC4085988&blobtype=pdf
info:eu-repo/semantics/altIdentifier/issn/1465-2080
info:eu-repo/semantics/altIdentifier/pmid/23475948
info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.064345-0
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
869-879
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
_version_ 1844616115973521408
score 13.070432

Publicaciones similares