BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis

Autores
Ruiz-Ranwez, V.; Posadas, D.M.; Van der Henst, C.; Estein, S.M.; Arocena, G.M.; Abdian, P.L.; Martín, F.A.; Sieira, R.; De Bolle, X.; Zorreguieta, A.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Brucella is responsible for brucellosis, one of the most common zoonoses worldwide that causes important economic losses in several countries. Increasing evidence indicates that adhesion of Brucella spp. to host cells is an important step to establish infection. We have previously shown that the BmaC unipolar monomeric autotransporter mediates the binding of Brucella suis to host cells through cell-associated fibronectin. Our genome analysis shows that the B. suis genome encodes several additional potential adhesins. In this work, we characterized a predicted trimeric autotransporter that we named BtaE. By expressing btaE in a nonadherent Escherichia coli strain and by phenotypic characterization of a B. suis δbtaE mutant, we showed that BtaE is involved in the binding of B. suis to hyaluronic acid. The B. suis δbtaE mutant exhibited a reduction in the adhesion to HeLa and A549 epithelial cells compared with the wild-type strain, and it was outcompeted by the wild-type strain in the binding to HeLa cells. The knockout btaE mutant showed an attenuated phenotype in the mouse model, indicating that BtaE is required for full virulence. BtaE was immunodetected on the bacterial surface at one cell pole. Using old and new pole markers, we observed that both the BmaC and BtaE adhesins are consistently associated with the new cell pole, suggesting that, in Brucella, the new pole is functionally differentiated for adhesion. This is consistent with the inherent polarization of this bacterium, and its role in the invasion process. © 2013, American Society for Microbiology.
Fil:Posadas, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Abdian, P.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Martín, F.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Infect. Immun. 2013;81(3):996-1007
Materia
adhesin
btae protein
fibronectin
hyaluronic acid
protein
unclassified drug
article
bacterial strain
bacterial virulence
bacterium adherence
Brucella suis
cell surface
computer model
epithelium cell
Escherichia coli
in vitro study
in vivo study
internalization
phenotype
priority journal
protein binding
protein expression
protein function
protein localization
Yersinia enterocolitica
Adhesins, Bacterial
Animals
Antibodies, Bacterial
Bacterial Adhesion
Brucella suis
Brucellosis
Carrier Proteins
Cell Polarity
Escherichia coli
Gene Expression Regulation, Bacterial
Mice
Mice, Inbred BALB C
Multigene Family
Virulence
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00199567_v81_n3_p996_RuizRanwez

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oai_identifier_str paperaa:paper_00199567_v81_n3_p996_RuizRanwez
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suisRuiz-Ranwez, V.Posadas, D.M.Van der Henst, C.Estein, S.M.Arocena, G.M.Abdian, P.L.Martín, F.A.Sieira, R.De Bolle, X.Zorreguieta, A.adhesinbtae proteinfibronectinhyaluronic acidproteinunclassified drugarticlebacterial strainbacterial virulencebacterium adherenceBrucella suiscell surfacecomputer modelepithelium cellEscherichia coliin vitro studyin vivo studyinternalizationphenotypepriority journalprotein bindingprotein expressionprotein functionprotein localizationYersinia enterocoliticaAdhesins, BacterialAnimalsAntibodies, BacterialBacterial AdhesionBrucella suisBrucellosisCarrier ProteinsCell PolarityEscherichia coliGene Expression Regulation, BacterialMiceMice, Inbred BALB CMultigene FamilyVirulenceBrucella is responsible for brucellosis, one of the most common zoonoses worldwide that causes important economic losses in several countries. Increasing evidence indicates that adhesion of Brucella spp. to host cells is an important step to establish infection. We have previously shown that the BmaC unipolar monomeric autotransporter mediates the binding of Brucella suis to host cells through cell-associated fibronectin. Our genome analysis shows that the B. suis genome encodes several additional potential adhesins. In this work, we characterized a predicted trimeric autotransporter that we named BtaE. By expressing btaE in a nonadherent Escherichia coli strain and by phenotypic characterization of a B. suis δbtaE mutant, we showed that BtaE is involved in the binding of B. suis to hyaluronic acid. The B. suis δbtaE mutant exhibited a reduction in the adhesion to HeLa and A549 epithelial cells compared with the wild-type strain, and it was outcompeted by the wild-type strain in the binding to HeLa cells. The knockout btaE mutant showed an attenuated phenotype in the mouse model, indicating that BtaE is required for full virulence. BtaE was immunodetected on the bacterial surface at one cell pole. Using old and new pole markers, we observed that both the BmaC and BtaE adhesins are consistently associated with the new cell pole, suggesting that, in Brucella, the new pole is functionally differentiated for adhesion. This is consistent with the inherent polarization of this bacterium, and its role in the invasion process. © 2013, American Society for Microbiology.Fil:Posadas, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Abdian, P.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Martín, F.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00199567_v81_n3_p996_RuizRanwezInfect. Immun. 2013;81(3):996-1007reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:09Zpaperaa:paper_00199567_v81_n3_p996_RuizRanwezInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:10.316Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
title BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
spellingShingle BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
Ruiz-Ranwez, V.
adhesin
btae protein
fibronectin
hyaluronic acid
protein
unclassified drug
article
bacterial strain
bacterial virulence
bacterium adherence
Brucella suis
cell surface
computer model
epithelium cell
Escherichia coli
in vitro study
in vivo study
internalization
phenotype
priority journal
protein binding
protein expression
protein function
protein localization
Yersinia enterocolitica
Adhesins, Bacterial
Animals
Antibodies, Bacterial
Bacterial Adhesion
Brucella suis
Brucellosis
Carrier Proteins
Cell Polarity
Escherichia coli
Gene Expression Regulation, Bacterial
Mice
Mice, Inbred BALB C
Multigene Family
Virulence
title_short BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
title_full BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
title_fullStr BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
title_full_unstemmed BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
title_sort BtaE, an adhesin that belongs to the trimeric autotransporter family, is required for full virulence and defines a specific adhesive pole of Brucella suis
dc.creator.none.fl_str_mv Ruiz-Ranwez, V.
Posadas, D.M.
Van der Henst, C.
Estein, S.M.
Arocena, G.M.
Abdian, P.L.
Martín, F.A.
Sieira, R.
De Bolle, X.
Zorreguieta, A.
author Ruiz-Ranwez, V.
author_facet Ruiz-Ranwez, V.
Posadas, D.M.
Van der Henst, C.
Estein, S.M.
Arocena, G.M.
Abdian, P.L.
Martín, F.A.
Sieira, R.
De Bolle, X.
Zorreguieta, A.
author_role author
author2 Posadas, D.M.
Van der Henst, C.
Estein, S.M.
Arocena, G.M.
Abdian, P.L.
Martín, F.A.
Sieira, R.
De Bolle, X.
Zorreguieta, A.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv adhesin
btae protein
fibronectin
hyaluronic acid
protein
unclassified drug
article
bacterial strain
bacterial virulence
bacterium adherence
Brucella suis
cell surface
computer model
epithelium cell
Escherichia coli
in vitro study
in vivo study
internalization
phenotype
priority journal
protein binding
protein expression
protein function
protein localization
Yersinia enterocolitica
Adhesins, Bacterial
Animals
Antibodies, Bacterial
Bacterial Adhesion
Brucella suis
Brucellosis
Carrier Proteins
Cell Polarity
Escherichia coli
Gene Expression Regulation, Bacterial
Mice
Mice, Inbred BALB C
Multigene Family
Virulence
topic adhesin
btae protein
fibronectin
hyaluronic acid
protein
unclassified drug
article
bacterial strain
bacterial virulence
bacterium adherence
Brucella suis
cell surface
computer model
epithelium cell
Escherichia coli
in vitro study
in vivo study
internalization
phenotype
priority journal
protein binding
protein expression
protein function
protein localization
Yersinia enterocolitica
Adhesins, Bacterial
Animals
Antibodies, Bacterial
Bacterial Adhesion
Brucella suis
Brucellosis
Carrier Proteins
Cell Polarity
Escherichia coli
Gene Expression Regulation, Bacterial
Mice
Mice, Inbred BALB C
Multigene Family
Virulence
dc.description.none.fl_txt_mv Brucella is responsible for brucellosis, one of the most common zoonoses worldwide that causes important economic losses in several countries. Increasing evidence indicates that adhesion of Brucella spp. to host cells is an important step to establish infection. We have previously shown that the BmaC unipolar monomeric autotransporter mediates the binding of Brucella suis to host cells through cell-associated fibronectin. Our genome analysis shows that the B. suis genome encodes several additional potential adhesins. In this work, we characterized a predicted trimeric autotransporter that we named BtaE. By expressing btaE in a nonadherent Escherichia coli strain and by phenotypic characterization of a B. suis δbtaE mutant, we showed that BtaE is involved in the binding of B. suis to hyaluronic acid. The B. suis δbtaE mutant exhibited a reduction in the adhesion to HeLa and A549 epithelial cells compared with the wild-type strain, and it was outcompeted by the wild-type strain in the binding to HeLa cells. The knockout btaE mutant showed an attenuated phenotype in the mouse model, indicating that BtaE is required for full virulence. BtaE was immunodetected on the bacterial surface at one cell pole. Using old and new pole markers, we observed that both the BmaC and BtaE adhesins are consistently associated with the new cell pole, suggesting that, in Brucella, the new pole is functionally differentiated for adhesion. This is consistent with the inherent polarization of this bacterium, and its role in the invasion process. © 2013, American Society for Microbiology.
Fil:Posadas, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Abdian, P.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Martín, F.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Brucella is responsible for brucellosis, one of the most common zoonoses worldwide that causes important economic losses in several countries. Increasing evidence indicates that adhesion of Brucella spp. to host cells is an important step to establish infection. We have previously shown that the BmaC unipolar monomeric autotransporter mediates the binding of Brucella suis to host cells through cell-associated fibronectin. Our genome analysis shows that the B. suis genome encodes several additional potential adhesins. In this work, we characterized a predicted trimeric autotransporter that we named BtaE. By expressing btaE in a nonadherent Escherichia coli strain and by phenotypic characterization of a B. suis δbtaE mutant, we showed that BtaE is involved in the binding of B. suis to hyaluronic acid. The B. suis δbtaE mutant exhibited a reduction in the adhesion to HeLa and A549 epithelial cells compared with the wild-type strain, and it was outcompeted by the wild-type strain in the binding to HeLa cells. The knockout btaE mutant showed an attenuated phenotype in the mouse model, indicating that BtaE is required for full virulence. BtaE was immunodetected on the bacterial surface at one cell pole. Using old and new pole markers, we observed that both the BmaC and BtaE adhesins are consistently associated with the new cell pole, suggesting that, in Brucella, the new pole is functionally differentiated for adhesion. This is consistent with the inherent polarization of this bacterium, and its role in the invasion process. © 2013, American Society for Microbiology.
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
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://hdl.handle.net/20.500.12110/paper_00199567_v81_n3_p996_RuizRanwez
url http://hdl.handle.net/20.500.12110/paper_00199567_v81_n3_p996_RuizRanwez
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Infect. Immun. 2013;81(3):996-1007
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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