The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components

Detalhes bibliográficos
Autor(a) principal: Magalhães,Caroline A
Data de Publicação: 2011
Outros Autores: Rossato,Sarita S, Barbosa,Ângela S, Santos,Thiago O dos, Elias,Waldir P, Sircili,Marcelo P, Piazza,Roxane MF
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=S0074-02762011000200005
Resumo: Typical and atypical enteropathogenic Escherichia coli (EPEC) are considered important bacterial causes of diarrhoea. Considering the repertoire of virulence genes, atypical EPEC (aEPEC) is a heterogeneous group, harbouring genes that are found in other diarrheagenic E. coli pathotypes, such as those encoding haemolysins. Haemolysins are cytolytic toxins that lyse host cells disrupting the function of the plasma membrane. In addition, these cytolysins mediate a connection to vascular tissue and/or blood components, such as plasma and cellular fibronectin. Therefore, we investigated the haemolytic activity of 72 aEPEC isolates and determined the correlation of this phenotype with the presence of genes encoding enterohaemolysins (Ehly) and cytolysin A (ClyA). In addition, the correlation between the expression of haemolysins and the ability of these secreted proteins to adhere to extracellular matrix (ECM) components was also assessed in this study. Our findings demonstrate that a subset of aEPEC presents haemolytic activity due to the expression of Ehlys and/or ClyA and that this activity is closely related to the ability of these isolates to bind to ECM components.
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spelling The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix componentsenteropathogenic Escherichia coliatypical EPECenterohaemolysinscytolysin Aextracellular matrix componentsTypical and atypical enteropathogenic Escherichia coli (EPEC) are considered important bacterial causes of diarrhoea. Considering the repertoire of virulence genes, atypical EPEC (aEPEC) is a heterogeneous group, harbouring genes that are found in other diarrheagenic E. coli pathotypes, such as those encoding haemolysins. Haemolysins are cytolytic toxins that lyse host cells disrupting the function of the plasma membrane. In addition, these cytolysins mediate a connection to vascular tissue and/or blood components, such as plasma and cellular fibronectin. Therefore, we investigated the haemolytic activity of 72 aEPEC isolates and determined the correlation of this phenotype with the presence of genes encoding enterohaemolysins (Ehly) and cytolysin A (ClyA). In addition, the correlation between the expression of haemolysins and the ability of these secreted proteins to adhere to extracellular matrix (ECM) components was also assessed in this study. Our findings demonstrate that a subset of aEPEC presents haemolytic activity due to the expression of Ehlys and/or ClyA and that this activity is closely related to the ability of these isolates to bind to ECM components.Instituto Oswaldo Cruz, Ministério da Saúde2011-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000200005Memórias do Instituto Oswaldo Cruz v.106 n.2 2011reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762011000200005info:eu-repo/semantics/openAccessMagalhães,Caroline ARossato,Sarita SBarbosa,Ângela SSantos,Thiago O dosElias,Waldir PSircili,Marcelo PPiazza,Roxane MFeng2020-04-25T17:50:57Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:17:29.872Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
title The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
spellingShingle The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
Magalhães,Caroline A
enteropathogenic Escherichia coli
atypical EPEC
enterohaemolysins
cytolysin A
extracellular matrix components
title_short The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
title_full The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
title_fullStr The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
title_full_unstemmed The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
title_sort The ability of haemolysins expressed by atypical enteropathogenic Escherichia coli to bind to extracellular matrix components
author Magalhães,Caroline A
author_facet Magalhães,Caroline A
Rossato,Sarita S
Barbosa,Ângela S
Santos,Thiago O dos
Elias,Waldir P
Sircili,Marcelo P
Piazza,Roxane MF
author_role author
author2 Rossato,Sarita S
Barbosa,Ângela S
Santos,Thiago O dos
Elias,Waldir P
Sircili,Marcelo P
Piazza,Roxane MF
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Magalhães,Caroline A
Rossato,Sarita S
Barbosa,Ângela S
Santos,Thiago O dos
Elias,Waldir P
Sircili,Marcelo P
Piazza,Roxane MF
dc.subject.por.fl_str_mv enteropathogenic Escherichia coli
atypical EPEC
enterohaemolysins
cytolysin A
extracellular matrix components
topic enteropathogenic Escherichia coli
atypical EPEC
enterohaemolysins
cytolysin A
extracellular matrix components
dc.description.none.fl_txt_mv Typical and atypical enteropathogenic Escherichia coli (EPEC) are considered important bacterial causes of diarrhoea. Considering the repertoire of virulence genes, atypical EPEC (aEPEC) is a heterogeneous group, harbouring genes that are found in other diarrheagenic E. coli pathotypes, such as those encoding haemolysins. Haemolysins are cytolytic toxins that lyse host cells disrupting the function of the plasma membrane. In addition, these cytolysins mediate a connection to vascular tissue and/or blood components, such as plasma and cellular fibronectin. Therefore, we investigated the haemolytic activity of 72 aEPEC isolates and determined the correlation of this phenotype with the presence of genes encoding enterohaemolysins (Ehly) and cytolysin A (ClyA). In addition, the correlation between the expression of haemolysins and the ability of these secreted proteins to adhere to extracellular matrix (ECM) components was also assessed in this study. Our findings demonstrate that a subset of aEPEC presents haemolytic activity due to the expression of Ehlys and/or ClyA and that this activity is closely related to the ability of these isolates to bind to ECM components.
description Typical and atypical enteropathogenic Escherichia coli (EPEC) are considered important bacterial causes of diarrhoea. Considering the repertoire of virulence genes, atypical EPEC (aEPEC) is a heterogeneous group, harbouring genes that are found in other diarrheagenic E. coli pathotypes, such as those encoding haemolysins. Haemolysins are cytolytic toxins that lyse host cells disrupting the function of the plasma membrane. In addition, these cytolysins mediate a connection to vascular tissue and/or blood components, such as plasma and cellular fibronectin. Therefore, we investigated the haemolytic activity of 72 aEPEC isolates and determined the correlation of this phenotype with the presence of genes encoding enterohaemolysins (Ehly) and cytolysin A (ClyA). In addition, the correlation between the expression of haemolysins and the ability of these secreted proteins to adhere to extracellular matrix (ECM) components was also assessed in this study. Our findings demonstrate that a subset of aEPEC presents haemolytic activity due to the expression of Ehlys and/or ClyA and that this activity is closely related to the ability of these isolates to bind to ECM components.
publishDate 2011
dc.date.none.fl_str_mv 2011-03-01
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=S0074-02762011000200005
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000200005
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-02762011000200005
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.106 n.2 2011
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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