BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells

Autores
Posadas, D.M.; Ruiz-Ranwez, V.; Bonomi, H.R.; Martín, F.A.; Zorreguieta, A.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Brucella is an intracellular pathogen responsible of a zoonotic disease called brucellosis. Brucella survives and proliferates within several types of phagocytic and non-phagocytic cells. Like in other pathogens, adhesion of brucellae to host surfaces was proposed to be an important step in the infection process. Indeed, Brucella has the capacity to bind to culture human cells and key components of the extracellular matrix, such as fibronectin. However, little is known about the molecular bases of Brucella adherence. In an attempt to identify bacterial genes encoding adhesins, a phage display library of Brucella suis was panned against fibronectin. Three fibronectin-binding proteins of B. suis were identified using this approach. One of the candidates, designated BmaC was a very large protein of 340kDa that is predicted to belong to the type I (monomeric) autotransporter family. Microscopy studies showed that BmaC is located at one pole on the bacterial surface. The phage displaying the fibronectin-binding peptide of BmaC inhibited the attachment of brucellae to both, HeLa cells and immobilized fibronectin in vitro. In addition, a bmaC deletion mutant was impaired in the ability of B. suis to attach to immobilized fibronectin and to the surface of HeLa and A549 cells and was out-competed by the wild-type strain in co-infection experiments. Finally, anti-fibronectin or anti-BmaC antibodies significantly inhibited the binding of wild-type bacteria to HeLa cells. Our results highlight the role of a novel monomeric autotransporter protein in the adhesion of B. suis to the extracellular matrix and non-phagocytic cells via fibronectin binding. © 2012 Blackwell Publishing Ltd.
Fil:Posadas, D.M. 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
Cell. Microbiol. 2012;14(6):965-982
Materia
bacterial protein
binding protein
bmac protein
fibronectin
unclassified drug
article
bacterial survival
bacterium adherence
Brucella suis
cell culture
controlled study
HeLa cell
host cell
human
human cell
in vitro study
nonhuman
priority journal
protein immobilization
Adhesins, Bacterial
Animals
Bacterial Adhesion
Brucella suis
Fibronectins
Gene Knockout Techniques
HeLa Cells
Host-Pathogen Interactions
Humans
Immobilized Proteins
Macrophages
Membrane Transport Proteins
Mice
Microbial Viability
Peptide Library
Protein Structure, Tertiary
Sequence Analysis, DNA
Bacteria (microorganisms)
Brucella
Brucella melitensis biovar Suis
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_14625814_v14_n6_p965_Posadas

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oai_identifier_str paperaa:paper_14625814_v14_n6_p965_Posadas
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cellsPosadas, D.M.Ruiz-Ranwez, V.Bonomi, H.R.Martín, F.A.Zorreguieta, A.bacterial proteinbinding proteinbmac proteinfibronectinunclassified drugarticlebacterial survivalbacterium adherenceBrucella suiscell culturecontrolled studyHeLa cellhost cellhumanhuman cellin vitro studynonhumanpriority journalprotein immobilizationAdhesins, BacterialAnimalsBacterial AdhesionBrucella suisFibronectinsGene Knockout TechniquesHeLa CellsHost-Pathogen InteractionsHumansImmobilized ProteinsMacrophagesMembrane Transport ProteinsMiceMicrobial ViabilityPeptide LibraryProtein Structure, TertiarySequence Analysis, DNABacteria (microorganisms)BrucellaBrucella melitensis biovar SuisBrucella is an intracellular pathogen responsible of a zoonotic disease called brucellosis. Brucella survives and proliferates within several types of phagocytic and non-phagocytic cells. Like in other pathogens, adhesion of brucellae to host surfaces was proposed to be an important step in the infection process. Indeed, Brucella has the capacity to bind to culture human cells and key components of the extracellular matrix, such as fibronectin. However, little is known about the molecular bases of Brucella adherence. In an attempt to identify bacterial genes encoding adhesins, a phage display library of Brucella suis was panned against fibronectin. Three fibronectin-binding proteins of B. suis were identified using this approach. One of the candidates, designated BmaC was a very large protein of 340kDa that is predicted to belong to the type I (monomeric) autotransporter family. Microscopy studies showed that BmaC is located at one pole on the bacterial surface. The phage displaying the fibronectin-binding peptide of BmaC inhibited the attachment of brucellae to both, HeLa cells and immobilized fibronectin in vitro. In addition, a bmaC deletion mutant was impaired in the ability of B. suis to attach to immobilized fibronectin and to the surface of HeLa and A549 cells and was out-competed by the wild-type strain in co-infection experiments. Finally, anti-fibronectin or anti-BmaC antibodies significantly inhibited the binding of wild-type bacteria to HeLa cells. Our results highlight the role of a novel monomeric autotransporter protein in the adhesion of B. suis to the extracellular matrix and non-phagocytic cells via fibronectin binding. © 2012 Blackwell Publishing Ltd.Fil:Posadas, D.M. 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.2012info: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_14625814_v14_n6_p965_PosadasCell. Microbiol. 2012;14(6):965-982reponame: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/ar2025-09-29T13:42:55Zpaperaa:paper_14625814_v14_n6_p965_PosadasInstitucionalhttps://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 13:42:56.303Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
title BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
spellingShingle BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
Posadas, D.M.
bacterial protein
binding protein
bmac protein
fibronectin
unclassified drug
article
bacterial survival
bacterium adherence
Brucella suis
cell culture
controlled study
HeLa cell
host cell
human
human cell
in vitro study
nonhuman
priority journal
protein immobilization
Adhesins, Bacterial
Animals
Bacterial Adhesion
Brucella suis
Fibronectins
Gene Knockout Techniques
HeLa Cells
Host-Pathogen Interactions
Humans
Immobilized Proteins
Macrophages
Membrane Transport Proteins
Mice
Microbial Viability
Peptide Library
Protein Structure, Tertiary
Sequence Analysis, DNA
Bacteria (microorganisms)
Brucella
Brucella melitensis biovar Suis
title_short BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
title_full BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
title_fullStr BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
title_full_unstemmed BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
title_sort BmaC, a novel autotransporter of Brucella suis, is involved in bacterial adhesion to host cells
dc.creator.none.fl_str_mv Posadas, D.M.
Ruiz-Ranwez, V.
Bonomi, H.R.
Martín, F.A.
Zorreguieta, A.
author Posadas, D.M.
author_facet Posadas, D.M.
Ruiz-Ranwez, V.
Bonomi, H.R.
Martín, F.A.
Zorreguieta, A.
author_role author
author2 Ruiz-Ranwez, V.
Bonomi, H.R.
Martín, F.A.
Zorreguieta, A.
author2_role author
author
author
author
dc.subject.none.fl_str_mv bacterial protein
binding protein
bmac protein
fibronectin
unclassified drug
article
bacterial survival
bacterium adherence
Brucella suis
cell culture
controlled study
HeLa cell
host cell
human
human cell
in vitro study
nonhuman
priority journal
protein immobilization
Adhesins, Bacterial
Animals
Bacterial Adhesion
Brucella suis
Fibronectins
Gene Knockout Techniques
HeLa Cells
Host-Pathogen Interactions
Humans
Immobilized Proteins
Macrophages
Membrane Transport Proteins
Mice
Microbial Viability
Peptide Library
Protein Structure, Tertiary
Sequence Analysis, DNA
Bacteria (microorganisms)
Brucella
Brucella melitensis biovar Suis
topic bacterial protein
binding protein
bmac protein
fibronectin
unclassified drug
article
bacterial survival
bacterium adherence
Brucella suis
cell culture
controlled study
HeLa cell
host cell
human
human cell
in vitro study
nonhuman
priority journal
protein immobilization
Adhesins, Bacterial
Animals
Bacterial Adhesion
Brucella suis
Fibronectins
Gene Knockout Techniques
HeLa Cells
Host-Pathogen Interactions
Humans
Immobilized Proteins
Macrophages
Membrane Transport Proteins
Mice
Microbial Viability
Peptide Library
Protein Structure, Tertiary
Sequence Analysis, DNA
Bacteria (microorganisms)
Brucella
Brucella melitensis biovar Suis
dc.description.none.fl_txt_mv Brucella is an intracellular pathogen responsible of a zoonotic disease called brucellosis. Brucella survives and proliferates within several types of phagocytic and non-phagocytic cells. Like in other pathogens, adhesion of brucellae to host surfaces was proposed to be an important step in the infection process. Indeed, Brucella has the capacity to bind to culture human cells and key components of the extracellular matrix, such as fibronectin. However, little is known about the molecular bases of Brucella adherence. In an attempt to identify bacterial genes encoding adhesins, a phage display library of Brucella suis was panned against fibronectin. Three fibronectin-binding proteins of B. suis were identified using this approach. One of the candidates, designated BmaC was a very large protein of 340kDa that is predicted to belong to the type I (monomeric) autotransporter family. Microscopy studies showed that BmaC is located at one pole on the bacterial surface. The phage displaying the fibronectin-binding peptide of BmaC inhibited the attachment of brucellae to both, HeLa cells and immobilized fibronectin in vitro. In addition, a bmaC deletion mutant was impaired in the ability of B. suis to attach to immobilized fibronectin and to the surface of HeLa and A549 cells and was out-competed by the wild-type strain in co-infection experiments. Finally, anti-fibronectin or anti-BmaC antibodies significantly inhibited the binding of wild-type bacteria to HeLa cells. Our results highlight the role of a novel monomeric autotransporter protein in the adhesion of B. suis to the extracellular matrix and non-phagocytic cells via fibronectin binding. © 2012 Blackwell Publishing Ltd.
Fil:Posadas, D.M. 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 an intracellular pathogen responsible of a zoonotic disease called brucellosis. Brucella survives and proliferates within several types of phagocytic and non-phagocytic cells. Like in other pathogens, adhesion of brucellae to host surfaces was proposed to be an important step in the infection process. Indeed, Brucella has the capacity to bind to culture human cells and key components of the extracellular matrix, such as fibronectin. However, little is known about the molecular bases of Brucella adherence. In an attempt to identify bacterial genes encoding adhesins, a phage display library of Brucella suis was panned against fibronectin. Three fibronectin-binding proteins of B. suis were identified using this approach. One of the candidates, designated BmaC was a very large protein of 340kDa that is predicted to belong to the type I (monomeric) autotransporter family. Microscopy studies showed that BmaC is located at one pole on the bacterial surface. The phage displaying the fibronectin-binding peptide of BmaC inhibited the attachment of brucellae to both, HeLa cells and immobilized fibronectin in vitro. In addition, a bmaC deletion mutant was impaired in the ability of B. suis to attach to immobilized fibronectin and to the surface of HeLa and A549 cells and was out-competed by the wild-type strain in co-infection experiments. Finally, anti-fibronectin or anti-BmaC antibodies significantly inhibited the binding of wild-type bacteria to HeLa cells. Our results highlight the role of a novel monomeric autotransporter protein in the adhesion of B. suis to the extracellular matrix and non-phagocytic cells via fibronectin binding. © 2012 Blackwell Publishing Ltd.
publishDate 2012
dc.date.none.fl_str_mv 2012
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_14625814_v14_n6_p965_Posadas
url http://hdl.handle.net/20.500.12110/paper_14625814_v14_n6_p965_Posadas
dc.language.none.fl_str_mv eng
language eng
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eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
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dc.source.none.fl_str_mv Cell. Microbiol. 2012;14(6):965-982
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
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