Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein secreted by pathogens and involved in adhesion and/or virulence. Previously we reported that enterohemorragic (EHEC) and enteropathogenic (EPEC) Escherichia coli secrete GAPDH into the culture medium. This bac...

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Autores: Aguilera Gil, Maria Laura, Ferreira, Elaine, Giménez Claudio, Rosa, Fernández Pérez, Francisco José, Taulés i Marín, Marta, Aguilar Piera, Juan, Vega Fernández, Maria Cristina, Badía Palacín, Josefa, Baldomà Llavinés, Laura
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2012
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/33549
Acceso en línea:https://hdl.handle.net/2445/33549
Access Level:acceso abierto
Palabra clave:Proteïnes
Escheríchia coli
Electroforesi
Transport biològic
Enterobacteriàcies
Proteins
Escherichia coli
Electrophoresis
Biological transport
Enterobacteriaceae
Seqüència d'aminoàcids
Amino acid sequence
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oai_identifier_str oai:recercat.cat:2445/33549
network_acronym_str ES
network_name_str España
repository_id_str
spelling Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coliAguilera Gil, Maria LauraFerreira, ElaineGiménez Claudio, RosaFernández Pérez, Francisco JoséTaulés i Marín, MartaAguilar Piera, JuanVega Fernández, Maria CristinaBadía Palacín, JosefaBaldomà Llavinés, LauraProteïnesEscheríchia coliElectroforesiTransport biològicEnterobacteriàciesProteinsEscherichia coliElectrophoresisBiological transportEnterobacteriaceaeSeqüència d'aminoàcidsAmino acid sequenceGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein secreted by pathogens and involved in adhesion and/or virulence. Previously we reported that enterohemorragic (EHEC) and enteropathogenic (EPEC) Escherichia coli secrete GAPDH into the culture medium. This bacterial protein binds human plasminogen and fibrinogen and remains associated with Caco-2 cells upon infection. In these pathogens, GAPDH secretion is not linked to outer membrane vesicles and depends on growth conditions, although the secretion mechanism is still unknown. EPEC is an attaching and effacing pathogen able to secrete and translocate multiple effector proteins into infected cells through a type III secretion system (T3SS). The secretion process is often dependent on a bacterial chaperone. The chaperone CesT displays broad substrate specificity and plays a central role in the recruitment of multiple type III effectors to the T3SS apparatus. Here we provide genetic evidences on GAPDH secretion through T3SS by EPEC grown in DMEM. Secretion of GAPDH is increased in sepD mutants and abolished in mutants defective in the type III ATPase EscN. Complementation with escN gene restores GAPDH secretion. In addition, we prove by means of pull down experiments, overlay immunoblotting and biolayer interferometry a novel interaction between GAPDH and the chaperone CesT. This interaction, which is strong and slow dissociating, may stabilise a population of GAPDH molecules in a secretion competent-state and target them to the type III secretion apparatus. This is the first description of CesT interaction with a housekeeping protein and its export through T3SS.Elsevier Ltd2013201320122013info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion8 p.application/pdfhttps://hdl.handle.net/2445/33549Articles publicats en revistes (Bioquímica i Biomedicina Molecular)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: http://dx.doi.org/10.1016/j.biocel.2012.03.002International Journal of Biochemistry and Cell Biology, 2012, vol. 44, núm. 6, p. 955-962http://dx.doi.org/10.1016/j.biocel.2012.03.002info:eu-repo/grantAgreement/EC/FP7/279039(c) Elsevier Ltd, 2012info:eu-repo/semantics/openAccessoai:recercat.cat:2445/335492026-05-29T05:05:01Z
dc.title.none.fl_str_mv Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
title Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
spellingShingle Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
Aguilera Gil, Maria Laura
Proteïnes
Escheríchia coli
Electroforesi
Transport biològic
Enterobacteriàcies
Proteins
Escherichia coli
Electrophoresis
Biological transport
Enterobacteriaceae
Seqüència d'aminoàcids
Amino acid sequence
title_short Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
title_full Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
title_fullStr Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
title_full_unstemmed Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
title_sort Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
dc.creator.none.fl_str_mv Aguilera Gil, Maria Laura
Ferreira, Elaine
Giménez Claudio, Rosa
Fernández Pérez, Francisco José
Taulés i Marín, Marta
Aguilar Piera, Juan
Vega Fernández, Maria Cristina
Badía Palacín, Josefa
Baldomà Llavinés, Laura
author Aguilera Gil, Maria Laura
author_facet Aguilera Gil, Maria Laura
Ferreira, Elaine
Giménez Claudio, Rosa
Fernández Pérez, Francisco José
Taulés i Marín, Marta
Aguilar Piera, Juan
Vega Fernández, Maria Cristina
Badía Palacín, Josefa
Baldomà Llavinés, Laura
author_role author
author2 Ferreira, Elaine
Giménez Claudio, Rosa
Fernández Pérez, Francisco José
Taulés i Marín, Marta
Aguilar Piera, Juan
Vega Fernández, Maria Cristina
Badía Palacín, Josefa
Baldomà Llavinés, Laura
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Proteïnes
Escheríchia coli
Electroforesi
Transport biològic
Enterobacteriàcies
Proteins
Escherichia coli
Electrophoresis
Biological transport
Enterobacteriaceae
Seqüència d'aminoàcids
Amino acid sequence
topic Proteïnes
Escheríchia coli
Electroforesi
Transport biològic
Enterobacteriàcies
Proteins
Escherichia coli
Electrophoresis
Biological transport
Enterobacteriaceae
Seqüència d'aminoàcids
Amino acid sequence
description Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein secreted by pathogens and involved in adhesion and/or virulence. Previously we reported that enterohemorragic (EHEC) and enteropathogenic (EPEC) Escherichia coli secrete GAPDH into the culture medium. This bacterial protein binds human plasminogen and fibrinogen and remains associated with Caco-2 cells upon infection. In these pathogens, GAPDH secretion is not linked to outer membrane vesicles and depends on growth conditions, although the secretion mechanism is still unknown. EPEC is an attaching and effacing pathogen able to secrete and translocate multiple effector proteins into infected cells through a type III secretion system (T3SS). The secretion process is often dependent on a bacterial chaperone. The chaperone CesT displays broad substrate specificity and plays a central role in the recruitment of multiple type III effectors to the T3SS apparatus. Here we provide genetic evidences on GAPDH secretion through T3SS by EPEC grown in DMEM. Secretion of GAPDH is increased in sepD mutants and abolished in mutants defective in the type III ATPase EscN. Complementation with escN gene restores GAPDH secretion. In addition, we prove by means of pull down experiments, overlay immunoblotting and biolayer interferometry a novel interaction between GAPDH and the chaperone CesT. This interaction, which is strong and slow dissociating, may stabilise a population of GAPDH molecules in a secretion competent-state and target them to the type III secretion apparatus. This is the first description of CesT interaction with a housekeeping protein and its export through T3SS.
publishDate 2012
dc.date.none.fl_str_mv 2012
2013
2013
2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/33549
url https://hdl.handle.net/2445/33549
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: http://dx.doi.org/10.1016/j.biocel.2012.03.002
International Journal of Biochemistry and Cell Biology, 2012, vol. 44, núm. 6, p. 955-962
http://dx.doi.org/10.1016/j.biocel.2012.03.002
info:eu-repo/grantAgreement/EC/FP7/279039
dc.rights.none.fl_str_mv (c) Elsevier Ltd, 2012
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Elsevier Ltd, 2012
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 8 p.
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ltd
publisher.none.fl_str_mv Elsevier Ltd
dc.source.none.fl_str_mv Articles publicats en revistes (Bioquímica i Biomedicina Molecular)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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