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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_14625814_v14_n6_p965_Posadas
Ver los metadatos del registro completo
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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 |
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 |
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 |
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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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ana@bl.fcen.uba.ar |
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