The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis

Detalhes bibliográficos
Autor(a) principal: Ferreira,Eliane de Oliveira
Data de Publicação: 2008
Outros Autores: Yates,Edwin Alexander, Goldner,Morris, Vommaro,Rossiane Cláudia, Silva Filho,Fernando Costa e, Petrópolis,Débora Barreiros, Domingues,Regina MC Pilotto
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000700010
Resumo: The Bacteroides fragilis ATCC strain was grown in a synthetic media with contrasting redox potential (Eh) levels [reduced (-60 mV) or oxidised (+100mV)] and their adhesion capacity to extracellular matrix components was evaluated. The strain was capable of adhering to laminin, fibronectin, fibronectin + heparan sulphate and heparan sulphate. A stronger adherence to laminin after growing the strain under oxidising conditions was verified. Electron microscopy using ruthenium red showed a heterogeneous population under this condition. Dot-blotting analyses confirmed stronger laminin recognition by outer membrane proteins of cells cultured at a higher Eh. Using a laminin affinity column, several putative laminin binding proteins obtained from the cultures kept under oxidising (60 kDa, 36 kDa, 25 kDa and 15 kDa) and reducing (60 kDa) conditions could be detected. Our results show that the expression of B. fragilis surface components that recognise laminin are influenced by Eh variations.
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spelling The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilisBacteroides fragilisadhesionredox potentiallaminin binding proteinsouter membrane proteinsThe Bacteroides fragilis ATCC strain was grown in a synthetic media with contrasting redox potential (Eh) levels [reduced (-60 mV) or oxidised (+100mV)] and their adhesion capacity to extracellular matrix components was evaluated. The strain was capable of adhering to laminin, fibronectin, fibronectin + heparan sulphate and heparan sulphate. A stronger adherence to laminin after growing the strain under oxidising conditions was verified. Electron microscopy using ruthenium red showed a heterogeneous population under this condition. Dot-blotting analyses confirmed stronger laminin recognition by outer membrane proteins of cells cultured at a higher Eh. Using a laminin affinity column, several putative laminin binding proteins obtained from the cultures kept under oxidising (60 kDa, 36 kDa, 25 kDa and 15 kDa) and reducing (60 kDa) conditions could be detected. Our results show that the expression of B. fragilis surface components that recognise laminin are influenced by Eh variations.Instituto Oswaldo Cruz, Ministério da Saúde2008-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000700010Memórias do Instituto Oswaldo Cruz v.103 n.7 2008reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762008000700010info:eu-repo/semantics/openAccessFerreira,Eliane de OliveiraYates,Edwin AlexanderGoldner,MorrisVommaro,Rossiane CláudiaSilva Filho,Fernando Costa ePetrópolis,Débora BarreirosDomingues,Regina MC Pilottoeng2020-04-25T17:50:22Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:15:49.206Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
title The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
spellingShingle The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
Ferreira,Eliane de Oliveira
Bacteroides fragilis
adhesion
redox potential
laminin binding proteins
outer membrane proteins
title_short The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
title_full The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
title_fullStr The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
title_full_unstemmed The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
title_sort The redox potential interferes with the expression of laminin binding molecules in Bacteroides fragilis
author Ferreira,Eliane de Oliveira
author_facet Ferreira,Eliane de Oliveira
Yates,Edwin Alexander
Goldner,Morris
Vommaro,Rossiane Cláudia
Silva Filho,Fernando Costa e
Petrópolis,Débora Barreiros
Domingues,Regina MC Pilotto
author_role author
author2 Yates,Edwin Alexander
Goldner,Morris
Vommaro,Rossiane Cláudia
Silva Filho,Fernando Costa e
Petrópolis,Débora Barreiros
Domingues,Regina MC Pilotto
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Ferreira,Eliane de Oliveira
Yates,Edwin Alexander
Goldner,Morris
Vommaro,Rossiane Cláudia
Silva Filho,Fernando Costa e
Petrópolis,Débora Barreiros
Domingues,Regina MC Pilotto
dc.subject.por.fl_str_mv Bacteroides fragilis
adhesion
redox potential
laminin binding proteins
outer membrane proteins
topic Bacteroides fragilis
adhesion
redox potential
laminin binding proteins
outer membrane proteins
dc.description.none.fl_txt_mv The Bacteroides fragilis ATCC strain was grown in a synthetic media with contrasting redox potential (Eh) levels [reduced (-60 mV) or oxidised (+100mV)] and their adhesion capacity to extracellular matrix components was evaluated. The strain was capable of adhering to laminin, fibronectin, fibronectin + heparan sulphate and heparan sulphate. A stronger adherence to laminin after growing the strain under oxidising conditions was verified. Electron microscopy using ruthenium red showed a heterogeneous population under this condition. Dot-blotting analyses confirmed stronger laminin recognition by outer membrane proteins of cells cultured at a higher Eh. Using a laminin affinity column, several putative laminin binding proteins obtained from the cultures kept under oxidising (60 kDa, 36 kDa, 25 kDa and 15 kDa) and reducing (60 kDa) conditions could be detected. Our results show that the expression of B. fragilis surface components that recognise laminin are influenced by Eh variations.
description The Bacteroides fragilis ATCC strain was grown in a synthetic media with contrasting redox potential (Eh) levels [reduced (-60 mV) or oxidised (+100mV)] and their adhesion capacity to extracellular matrix components was evaluated. The strain was capable of adhering to laminin, fibronectin, fibronectin + heparan sulphate and heparan sulphate. A stronger adherence to laminin after growing the strain under oxidising conditions was verified. Electron microscopy using ruthenium red showed a heterogeneous population under this condition. Dot-blotting analyses confirmed stronger laminin recognition by outer membrane proteins of cells cultured at a higher Eh. Using a laminin affinity column, several putative laminin binding proteins obtained from the cultures kept under oxidising (60 kDa, 36 kDa, 25 kDa and 15 kDa) and reducing (60 kDa) conditions could be detected. Our results show that the expression of B. fragilis surface components that recognise laminin are influenced by Eh variations.
publishDate 2008
dc.date.none.fl_str_mv 2008-11-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000700010
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762008000700010
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-02762008000700010
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.103 n.7 2008
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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