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
- 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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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 |
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Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
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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 |
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