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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/53344
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/53344 |
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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 Técnicas2025-09-29T10:24:47Zoai: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:34982025-09-29 10:24:47.561CONICET 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 |
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CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
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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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1844614245108416512 |
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13.070432 |