Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake

Autores
Sauvageot, Nicolas; Mokhtari, Abdelhamid; Joyet, Philippe; Budin Verneuil, Aurélie; Blancato, Victor Sebastian; Repizo, Guillermo Daniel; Henry, Céline; Pikis, Andreas; Thompson, John; Magni, Christian; Hartke, Axel; Deutscher, Josef
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Maltodextrin is a mixture of maltooligosaccharides, which are produced by the degradation of starch or glycogen. They are mostly composed of α-1,4- and some α-1,6-linked glucose residues. Genes presumed to code for the Enterococcus faecalis maltodextrin transporter were induced during enterococcal infection. We therefore carried out a detailed study of maltodextrin transport in this organism. Depending on their length (3 to 7 glucose residues), E. faecalis takes up maltodextrins either via MalT, a maltose-specific permease of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS), or the ATP binding cassette (ABC) transporter MdxEFG-MsmX. Maltotriose, the smallest maltodextrin, is primarily transported by the PTS permease. A malT mutant therefore exhibits significantly reduced growth on maltose and maltotriose. The residual uptake of the trisaccharide is catalyzed by the ABC transporter, because a malT mdxF double mutant no longer grows on maltotriose. The trisaccharide arrives as maltotriose-6"-P in the cell. MapP, which dephosphorylates maltose-6'-P, also releases Pi from maltotriose-6"-P. Maltotetraose and longer maltodextrins are mainly (or exclusively) taken up via the ABC transporter, because inactivation of the membrane protein MdxF prevents growth on maltotetraose and longer maltodextrins up to at least maltoheptaose. E. faecalis also utilizes panose and isopanose, and we show for the first time, to our knowledge, that in contrast to maltotriose, its two isomers are primarily transported via the ABC transporter. We confirm that maltodextrin utilization via MdxEFG-MsmX affects the colonization capacity of E. faecalis, because inactivation of mdxF significantly reduced enterococcal colonization and/or survival in kidneys and liver of mice after intraperitoneal infection.
Fil: Sauvageot, Nicolas. Universite de Caen Basse Normandie; Francia
Fil: Mokhtari, Abdelhamid. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia. 8 May 1945 University of Guelma; Argelia
Fil: Joyet, Philippe. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Budin Verneuil, Aurélie. Universite de Caen Basse Normandie; Francia
Fil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Henry, Céline. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Pikis, Andreas. National Institutes of Health; Estados Unidos. Center for Drug Evaluation and Research, Food and Drug Administration; Estados Unidos
Fil: Thompson, John. National Institutes of Health; Estados Unidos
Fil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Hartke, Axel. Universite de Caen Basse Normandie; Francia
Fil: Deutscher, Josef. Institut National de la Recherche Agronomique; Francia. Université Paris-Saclay; Francia. Centre National de la Recherche Scientifique; Francia. Université Paris Diderot - Paris 7; Francia
Materia
ABC TRANSPORTER
ENTEROCOCCI
HOST COLONIZATION
MALTODEXTRIN
PHOSPHOTRANSFERASE SYSTEM
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/53344
Acceder
id CONICETDig_a4783d99048684727cc120b7923cfd8a
oai_identifier_str oai:ri.conicet.gov.ar:11336/53344
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptakeSauvageot, NicolasMokhtari, AbdelhamidJoyet, PhilippeBudin Verneuil, AurélieBlancato, Victor SebastianRepizo, Guillermo DanielHenry, CélinePikis, AndreasThompson, JohnMagni, ChristianHartke, AxelDeutscher, JosefABC TRANSPORTERENTEROCOCCIHOST COLONIZATIONMALTODEXTRINPHOSPHOTRANSFERASE SYSTEMhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Maltodextrin is a mixture of maltooligosaccharides, which are produced by the degradation of starch or glycogen. They are mostly composed of α-1,4- and some α-1,6-linked glucose residues. Genes presumed to code for the Enterococcus faecalis maltodextrin transporter were induced during enterococcal infection. We therefore carried out a detailed study of maltodextrin transport in this organism. Depending on their length (3 to 7 glucose residues), E. faecalis takes up maltodextrins either via MalT, a maltose-specific permease of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS), or the ATP binding cassette (ABC) transporter MdxEFG-MsmX. Maltotriose, the smallest maltodextrin, is primarily transported by the PTS permease. A malT mutant therefore exhibits significantly reduced growth on maltose and maltotriose. The residual uptake of the trisaccharide is catalyzed by the ABC transporter, because a malT mdxF double mutant no longer grows on maltotriose. The trisaccharide arrives as maltotriose-6"-P in the cell. MapP, which dephosphorylates maltose-6'-P, also releases Pi from maltotriose-6"-P. Maltotetraose and longer maltodextrins are mainly (or exclusively) taken up via the ABC transporter, because inactivation of the membrane protein MdxF prevents growth on maltotetraose and longer maltodextrins up to at least maltoheptaose. E. faecalis also utilizes panose and isopanose, and we show for the first time, to our knowledge, that in contrast to maltotriose, its two isomers are primarily transported via the ABC transporter. We confirm that maltodextrin utilization via MdxEFG-MsmX affects the colonization capacity of E. faecalis, because inactivation of mdxF significantly reduced enterococcal colonization and/or survival in kidneys and liver of mice after intraperitoneal infection.Fil: Sauvageot, Nicolas. Universite de Caen Basse Normandie; FranciaFil: Mokhtari, Abdelhamid. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia. 8 May 1945 University of Guelma; ArgeliaFil: Joyet, Philippe. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; FranciaFil: Budin Verneuil, Aurélie. Universite de Caen Basse Normandie; FranciaFil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Henry, Céline. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; FranciaFil: Pikis, Andreas. National Institutes of Health; Estados Unidos. Center for Drug Evaluation and Research, Food and Drug Administration; Estados UnidosFil: Thompson, John. National Institutes of Health; Estados UnidosFil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Hartke, Axel. Universite de Caen Basse Normandie; FranciaFil: Deutscher, Josef. Institut National de la Recherche Agronomique; Francia. Université Paris-Saclay; Francia. Centre National de la Recherche Scientifique; Francia. Université Paris Diderot - Paris 7; FranciaAmerican Society for Microbiology2017-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/53344Sauvageot, Nicolas; Mokhtari, Abdelhamid; Joyet, Philippe; Budin Verneuil, Aurélie; Blancato, Victor Sebastian; et al.; Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake; American Society for Microbiology; Journal of Bacteriology; 199; 9; 5-2017; 1-490021-9193CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/JB.00878-16info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388810/info:eu-repo/semantics/altIdentifier/url/http://jb.asm.org/content/199/9/e00878-16.longinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:57:31Zoai:ri.conicet.gov.ar:11336/53344instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:57:31.345CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
title Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
spellingShingle Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
Sauvageot, Nicolas
ABC TRANSPORTER
ENTEROCOCCI
HOST COLONIZATION
MALTODEXTRIN
PHOSPHOTRANSFERASE SYSTEM
title_short Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
title_full Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
title_fullStr Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
title_full_unstemmed Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
title_sort Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake
dc.creator.none.fl_str_mv Sauvageot, Nicolas
Mokhtari, Abdelhamid
Joyet, Philippe
Budin Verneuil, Aurélie
Blancato, Victor Sebastian
Repizo, Guillermo Daniel
Henry, Céline
Pikis, Andreas
Thompson, John
Magni, Christian
Hartke, Axel
Deutscher, Josef
author Sauvageot, Nicolas
author_facet Sauvageot, Nicolas
Mokhtari, Abdelhamid
Joyet, Philippe
Budin Verneuil, Aurélie
Blancato, Victor Sebastian
Repizo, Guillermo Daniel
Henry, Céline
Pikis, Andreas
Thompson, John
Magni, Christian
Hartke, Axel
Deutscher, Josef
author_role author
author2 Mokhtari, Abdelhamid
Joyet, Philippe
Budin Verneuil, Aurélie
Blancato, Victor Sebastian
Repizo, Guillermo Daniel
Henry, Céline
Pikis, Andreas
Thompson, John
Magni, Christian
Hartke, Axel
Deutscher, Josef
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ABC TRANSPORTER
ENTEROCOCCI
HOST COLONIZATION
MALTODEXTRIN
PHOSPHOTRANSFERASE SYSTEM
topic ABC TRANSPORTER
ENTEROCOCCI
HOST COLONIZATION
MALTODEXTRIN
PHOSPHOTRANSFERASE SYSTEM
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Maltodextrin is a mixture of maltooligosaccharides, which are produced by the degradation of starch or glycogen. They are mostly composed of α-1,4- and some α-1,6-linked glucose residues. Genes presumed to code for the Enterococcus faecalis maltodextrin transporter were induced during enterococcal infection. We therefore carried out a detailed study of maltodextrin transport in this organism. Depending on their length (3 to 7 glucose residues), E. faecalis takes up maltodextrins either via MalT, a maltose-specific permease of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS), or the ATP binding cassette (ABC) transporter MdxEFG-MsmX. Maltotriose, the smallest maltodextrin, is primarily transported by the PTS permease. A malT mutant therefore exhibits significantly reduced growth on maltose and maltotriose. The residual uptake of the trisaccharide is catalyzed by the ABC transporter, because a malT mdxF double mutant no longer grows on maltotriose. The trisaccharide arrives as maltotriose-6"-P in the cell. MapP, which dephosphorylates maltose-6'-P, also releases Pi from maltotriose-6"-P. Maltotetraose and longer maltodextrins are mainly (or exclusively) taken up via the ABC transporter, because inactivation of the membrane protein MdxF prevents growth on maltotetraose and longer maltodextrins up to at least maltoheptaose. E. faecalis also utilizes panose and isopanose, and we show for the first time, to our knowledge, that in contrast to maltotriose, its two isomers are primarily transported via the ABC transporter. We confirm that maltodextrin utilization via MdxEFG-MsmX affects the colonization capacity of E. faecalis, because inactivation of mdxF significantly reduced enterococcal colonization and/or survival in kidneys and liver of mice after intraperitoneal infection.
Fil: Sauvageot, Nicolas. Universite de Caen Basse Normandie; Francia
Fil: Mokhtari, Abdelhamid. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia. 8 May 1945 University of Guelma; Argelia
Fil: Joyet, Philippe. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Budin Verneuil, Aurélie. Universite de Caen Basse Normandie; Francia
Fil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Henry, Céline. Université Paris-Saclay; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Pikis, Andreas. National Institutes of Health; Estados Unidos. Center for Drug Evaluation and Research, Food and Drug Administration; Estados Unidos
Fil: Thompson, John. National Institutes of Health; Estados Unidos
Fil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Hartke, Axel. Universite de Caen Basse Normandie; Francia
Fil: Deutscher, Josef. Institut National de la Recherche Agronomique; Francia. Université Paris-Saclay; Francia. Centre National de la Recherche Scientifique; Francia. Université Paris Diderot - Paris 7; Francia
description Maltodextrin is a mixture of maltooligosaccharides, which are produced by the degradation of starch or glycogen. They are mostly composed of α-1,4- and some α-1,6-linked glucose residues. Genes presumed to code for the Enterococcus faecalis maltodextrin transporter were induced during enterococcal infection. We therefore carried out a detailed study of maltodextrin transport in this organism. Depending on their length (3 to 7 glucose residues), E. faecalis takes up maltodextrins either via MalT, a maltose-specific permease of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS), or the ATP binding cassette (ABC) transporter MdxEFG-MsmX. Maltotriose, the smallest maltodextrin, is primarily transported by the PTS permease. A malT mutant therefore exhibits significantly reduced growth on maltose and maltotriose. The residual uptake of the trisaccharide is catalyzed by the ABC transporter, because a malT mdxF double mutant no longer grows on maltotriose. The trisaccharide arrives as maltotriose-6"-P in the cell. MapP, which dephosphorylates maltose-6'-P, also releases Pi from maltotriose-6"-P. Maltotetraose and longer maltodextrins are mainly (or exclusively) taken up via the ABC transporter, because inactivation of the membrane protein MdxF prevents growth on maltotetraose and longer maltodextrins up to at least maltoheptaose. E. faecalis also utilizes panose and isopanose, and we show for the first time, to our knowledge, that in contrast to maltotriose, its two isomers are primarily transported via the ABC transporter. We confirm that maltodextrin utilization via MdxEFG-MsmX affects the colonization capacity of E. faecalis, because inactivation of mdxF significantly reduced enterococcal colonization and/or survival in kidneys and liver of mice after intraperitoneal infection.
publishDate 2017
dc.date.none.fl_str_mv 2017-05
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/11336/53344
Sauvageot, Nicolas; Mokhtari, Abdelhamid; Joyet, Philippe; Budin Verneuil, Aurélie; Blancato, Victor Sebastian; et al.; Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake; American Society for Microbiology; Journal of Bacteriology; 199; 9; 5-2017; 1-49
0021-9193
CONICET Digital
CONICET
url http://hdl.handle.net/11336/53344
identifier_str_mv Sauvageot, Nicolas; Mokhtari, Abdelhamid; Joyet, Philippe; Budin Verneuil, Aurélie; Blancato, Victor Sebastian; et al.; Enterococcus faecalis uses a phosphotransferase system permease and a host colonization-related ABC transporter for maltodextrin uptake; American Society for Microbiology; Journal of Bacteriology; 199; 9; 5-2017; 1-49
0021-9193
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1128/JB.00878-16
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388810/
info:eu-repo/semantics/altIdentifier/url/http://jb.asm.org/content/199/9/e00878-16.long
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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