Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum

Autores
Sanz, Silvia; Bandini, Giulia; Ospina, Diego; Bernabeu, Maria; Mariño, Karina Valeria; Fernández Becerra, Carmen; Izquierdo, Luis
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Carbohydrate structures play important roles in many biological processes, including cell adhesion, cell-cell communication, and host-pathogen interactions. Sugar nucleotides are activated forms of sugars used by the cell as donors for most glycosylation reactions. Using a liquid chromatography-tandem mass spectrometry- based method, we identified and quantified the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plasmodium falciparum intraerythrocytic life stages. We assembled these data with the in silico functional reconstruction of the parasite metabolic pathways obtained from the P. falciparum annotated genome, exposing new active biosynthetic routes crucial for further glycosylation reactions. Fucose is a sugar present in glycoconjugates often associated with recognition and adhesion events. Thus, the GDP-fucose precursor is essential in a wide variety of organisms. P. falciparum presents homologues of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase enzymes that are active in vitro, indicating that most GDP-fucose is formed by a de novo pathway that involves the bioconversion of GDP-mannose. Homologues for enzymes involved in a fucose salvage pathway are apparently absent in the P. falciparum genome. This is in agreement with in vivo metabolic labeling experiments showing that fucose is not significantly incorporated by the parasite. Fluorescence microscopy of epitope-tagged versions of P. falciparum GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase expressed in transgenic 3D7 parasites shows that these enzymes localize in the cytoplasm of P. falciparum during the intraerythrocytic developmental cycle. Although the function of fucose in the parasite is not known, the presence of GDPfucose suggests that the metabolite may be used for further fucosylation reactions.
Fil: Sanz, Silvia. Universidad de Barcelona; España
Fil: Bandini, Giulia. Boston University; Estados Unidos
Fil: Ospina, Diego. Universidad de Barcelona; España
Fil: Bernabeu, Maria. Universidad de Barcelona; España
Fil: Mariño, Karina Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Fernández Becerra, Carmen. Universidad de Barcelona; España
Fil: Izquierdo, Luis. Universidad de Barcelona; España
Materia
Sugar Nucleotides
Malaria
Plasmodium Falciparum
Glycobiology
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:11336/2357
Acceder
id CONICETDig_80a8d144cdf18578fbe3522160c6e8dd
oai_identifier_str oai:ri.conicet.gov.ar:11336/2357
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparumSanz, SilviaBandini, GiuliaOspina, DiegoBernabeu, MariaMariño, Karina ValeriaFernández Becerra, CarmenIzquierdo, LuisSugar NucleotidesMalariaPlasmodium FalciparumGlycobiologyhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Carbohydrate structures play important roles in many biological processes, including cell adhesion, cell-cell communication, and host-pathogen interactions. Sugar nucleotides are activated forms of sugars used by the cell as donors for most glycosylation reactions. Using a liquid chromatography-tandem mass spectrometry- based method, we identified and quantified the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plasmodium falciparum intraerythrocytic life stages. We assembled these data with the in silico functional reconstruction of the parasite metabolic pathways obtained from the P. falciparum annotated genome, exposing new active biosynthetic routes crucial for further glycosylation reactions. Fucose is a sugar present in glycoconjugates often associated with recognition and adhesion events. Thus, the GDP-fucose precursor is essential in a wide variety of organisms. P. falciparum presents homologues of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase enzymes that are active in vitro, indicating that most GDP-fucose is formed by a de novo pathway that involves the bioconversion of GDP-mannose. Homologues for enzymes involved in a fucose salvage pathway are apparently absent in the P. falciparum genome. This is in agreement with in vivo metabolic labeling experiments showing that fucose is not significantly incorporated by the parasite. Fluorescence microscopy of epitope-tagged versions of P. falciparum GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase expressed in transgenic 3D7 parasites shows that these enzymes localize in the cytoplasm of P. falciparum during the intraerythrocytic developmental cycle. Although the function of fucose in the parasite is not known, the presence of GDPfucose suggests that the metabolite may be used for further fucosylation reactions.Fil: Sanz, Silvia. Universidad de Barcelona; EspañaFil: Bandini, Giulia. Boston University; Estados UnidosFil: Ospina, Diego. Universidad de Barcelona; EspañaFil: Bernabeu, Maria. Universidad de Barcelona; EspañaFil: Mariño, Karina Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaFil: Fernández Becerra, Carmen. Universidad de Barcelona; EspañaFil: Izquierdo, Luis. Universidad de Barcelona; EspañaAmerican Society for Biochemistry and Molecular Biology2013-06-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/2357Sanz, Silvia; Bandini, Giulia; Ospina, Diego; Bernabeu, Maria; Mariño, Karina Valeria; et al.; Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 288; 23; 7-6-2013; 16506-165170021-92581083-351Xenginfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M112.439828info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/288/23/16506.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 Técnicas2025-09-29T09:46:27Zoai:ri.conicet.gov.ar:11336/2357instacron: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 09:46:27.448CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
title Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
spellingShingle Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
Sanz, Silvia
Sugar Nucleotides
Malaria
Plasmodium Falciparum
Glycobiology
title_short Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
title_full Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
title_fullStr Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
title_full_unstemmed Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
title_sort Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum
dc.creator.none.fl_str_mv Sanz, Silvia
Bandini, Giulia
Ospina, Diego
Bernabeu, Maria
Mariño, Karina Valeria
Fernández Becerra, Carmen
Izquierdo, Luis
author Sanz, Silvia
author_facet Sanz, Silvia
Bandini, Giulia
Ospina, Diego
Bernabeu, Maria
Mariño, Karina Valeria
Fernández Becerra, Carmen
Izquierdo, Luis
author_role author
author2 Bandini, Giulia
Ospina, Diego
Bernabeu, Maria
Mariño, Karina Valeria
Fernández Becerra, Carmen
Izquierdo, Luis
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Sugar Nucleotides
Malaria
Plasmodium Falciparum
Glycobiology
topic Sugar Nucleotides
Malaria
Plasmodium Falciparum
Glycobiology
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Carbohydrate structures play important roles in many biological processes, including cell adhesion, cell-cell communication, and host-pathogen interactions. Sugar nucleotides are activated forms of sugars used by the cell as donors for most glycosylation reactions. Using a liquid chromatography-tandem mass spectrometry- based method, we identified and quantified the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plasmodium falciparum intraerythrocytic life stages. We assembled these data with the in silico functional reconstruction of the parasite metabolic pathways obtained from the P. falciparum annotated genome, exposing new active biosynthetic routes crucial for further glycosylation reactions. Fucose is a sugar present in glycoconjugates often associated with recognition and adhesion events. Thus, the GDP-fucose precursor is essential in a wide variety of organisms. P. falciparum presents homologues of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase enzymes that are active in vitro, indicating that most GDP-fucose is formed by a de novo pathway that involves the bioconversion of GDP-mannose. Homologues for enzymes involved in a fucose salvage pathway are apparently absent in the P. falciparum genome. This is in agreement with in vivo metabolic labeling experiments showing that fucose is not significantly incorporated by the parasite. Fluorescence microscopy of epitope-tagged versions of P. falciparum GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase expressed in transgenic 3D7 parasites shows that these enzymes localize in the cytoplasm of P. falciparum during the intraerythrocytic developmental cycle. Although the function of fucose in the parasite is not known, the presence of GDPfucose suggests that the metabolite may be used for further fucosylation reactions.
Fil: Sanz, Silvia. Universidad de Barcelona; España
Fil: Bandini, Giulia. Boston University; Estados Unidos
Fil: Ospina, Diego. Universidad de Barcelona; España
Fil: Bernabeu, Maria. Universidad de Barcelona; España
Fil: Mariño, Karina Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Fernández Becerra, Carmen. Universidad de Barcelona; España
Fil: Izquierdo, Luis. Universidad de Barcelona; España
description Carbohydrate structures play important roles in many biological processes, including cell adhesion, cell-cell communication, and host-pathogen interactions. Sugar nucleotides are activated forms of sugars used by the cell as donors for most glycosylation reactions. Using a liquid chromatography-tandem mass spectrometry- based method, we identified and quantified the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plasmodium falciparum intraerythrocytic life stages. We assembled these data with the in silico functional reconstruction of the parasite metabolic pathways obtained from the P. falciparum annotated genome, exposing new active biosynthetic routes crucial for further glycosylation reactions. Fucose is a sugar present in glycoconjugates often associated with recognition and adhesion events. Thus, the GDP-fucose precursor is essential in a wide variety of organisms. P. falciparum presents homologues of GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase enzymes that are active in vitro, indicating that most GDP-fucose is formed by a de novo pathway that involves the bioconversion of GDP-mannose. Homologues for enzymes involved in a fucose salvage pathway are apparently absent in the P. falciparum genome. This is in agreement with in vivo metabolic labeling experiments showing that fucose is not significantly incorporated by the parasite. Fluorescence microscopy of epitope-tagged versions of P. falciparum GDP-mannose 4,6-dehydratase and GDP-L-fucose synthase expressed in transgenic 3D7 parasites shows that these enzymes localize in the cytoplasm of P. falciparum during the intraerythrocytic developmental cycle. Although the function of fucose in the parasite is not known, the presence of GDPfucose suggests that the metabolite may be used for further fucosylation reactions.
publishDate 2013
dc.date.none.fl_str_mv 2013-06-07
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/11336/2357
Sanz, Silvia; Bandini, Giulia; Ospina, Diego; Bernabeu, Maria; Mariño, Karina Valeria; et al.; Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 288; 23; 7-6-2013; 16506-16517
0021-9258
1083-351X
url http://hdl.handle.net/11336/2357
identifier_str_mv Sanz, Silvia; Bandini, Giulia; Ospina, Diego; Bernabeu, Maria; Mariño, Karina Valeria; et al.; Biosynthesis of GDP-fucose and other sugar nucleotides in the blood-stages of Plasmodium falciparum; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 288; 23; 7-6-2013; 16506-16517
0021-9258
1083-351X
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M112.439828
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/288/23/16506.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 Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
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 13.070432

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