Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface

Autores
Silva Alvarez, Maria Valeria; Folle, Ana Maite; Ramos, Ana Lía; Zamarreño, Fernando; Costabel, Marcelo Daniel; García Zepeda, Eduardo; Salinas, Gustavo; Córsico, Betina; Ferreira, Ana María
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipids are mainly solubilized by various families of lipid binding proteins which participate in their transport between tissues as well as cell compartments. Among these families, Hydrophobic Ligand Binding Proteins (HLBPs) deserve special consideration since they comprise intracellular and extracellular members, are able to bind a variety of fatty acids, retinoids and some sterols, and are present exclusively in cestodes. Since these parasites have lost catabolic and biosynthetic pathways for fatty acids and cholesterol, HLBPs are likely relevant for lipid uptake and transportation between parasite and host cells. Echinococcus granulosus antigen B (EgAgB) is a lipoprotein belonging to the HLBP family, which is very abundant in the larval stage of this parasite. Herein, we review the literature on EgAgB composition, structural organization and biological properties, and propose an integrated scenario in which this parasite HLBP contributes to adaptation to mammalian hosts by meeting both metabolic and immunomodulatory parasite demands.
Fil: Silva Alvarez, Maria Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Folle, Ana Maite. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Ramos, Ana Lía. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur; Argentina
Fil: García Zepeda, Eduardo. Universidad Nacional Autónoma de México; México
Fil: Salinas, Gustavo. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina
Fil: Ferreira, Ana María. Universidad del Uruguay. Facultad de Ciencias; Uruguay
Materia
Cestode
Echinococcus
Hlbp
Lipoprotein
Antigen B
Tapeworm
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:11336/39626
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/39626
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interfaceSilva Alvarez, Maria ValeriaFolle, Ana MaiteRamos, Ana LíaZamarreño, FernandoCostabel, Marcelo DanielGarcía Zepeda, EduardoSalinas, GustavoCórsico, BetinaFerreira, Ana MaríaCestodeEchinococcusHlbpLipoproteinAntigen BTapewormhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Lipids are mainly solubilized by various families of lipid binding proteins which participate in their transport between tissues as well as cell compartments. Among these families, Hydrophobic Ligand Binding Proteins (HLBPs) deserve special consideration since they comprise intracellular and extracellular members, are able to bind a variety of fatty acids, retinoids and some sterols, and are present exclusively in cestodes. Since these parasites have lost catabolic and biosynthetic pathways for fatty acids and cholesterol, HLBPs are likely relevant for lipid uptake and transportation between parasite and host cells. Echinococcus granulosus antigen B (EgAgB) is a lipoprotein belonging to the HLBP family, which is very abundant in the larval stage of this parasite. Herein, we review the literature on EgAgB composition, structural organization and biological properties, and propose an integrated scenario in which this parasite HLBP contributes to adaptation to mammalian hosts by meeting both metabolic and immunomodulatory parasite demands.Fil: Silva Alvarez, Maria Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina. Universidad de la República. Facultad de Ciencias; UruguayFil: Folle, Ana Maite. Universidad de la República. Facultad de Ciencias; UruguayFil: Ramos, Ana Lía. Universidad de la República. Facultad de Ciencias; UruguayFil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Costabel, Marcelo Daniel. Universidad Nacional del Sur; ArgentinaFil: García Zepeda, Eduardo. Universidad Nacional Autónoma de México; MéxicoFil: Salinas, Gustavo. Universidad de la República. Facultad de Ciencias; UruguayFil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; ArgentinaFil: Ferreira, Ana María. Universidad del Uruguay. Facultad de Ciencias; UruguayElsevier2015-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39626Silva Alvarez, Maria Valeria; Folle, Ana Maite; Ramos, Ana Lía; Zamarreño, Fernando; Costabel, Marcelo Daniel; et al.; Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface; Elsevier; Prostaglandins Leukotrienes and Essential Fatty Acids; 93; 2-2015; 17-230952-3278CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.plefa.com/article/S0952-3278(14)00152-5/fulltextinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.plefa.2014.09.008info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0952327814001525info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:26:09Zoai:ri.conicet.gov.ar:11336/39626instacron: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 11:26:09.967CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
title Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
spellingShingle Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
Silva Alvarez, Maria Valeria
Cestode
Echinococcus
Hlbp
Lipoprotein
Antigen B
Tapeworm
title_short Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
title_full Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
title_fullStr Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
title_full_unstemmed Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
title_sort Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface
dc.creator.none.fl_str_mv Silva Alvarez, Maria Valeria
Folle, Ana Maite
Ramos, Ana Lía
Zamarreño, Fernando
Costabel, Marcelo Daniel
García Zepeda, Eduardo
Salinas, Gustavo
Córsico, Betina
Ferreira, Ana María
author Silva Alvarez, Maria Valeria
author_facet Silva Alvarez, Maria Valeria
Folle, Ana Maite
Ramos, Ana Lía
Zamarreño, Fernando
Costabel, Marcelo Daniel
García Zepeda, Eduardo
Salinas, Gustavo
Córsico, Betina
Ferreira, Ana María
author_role author
author2 Folle, Ana Maite
Ramos, Ana Lía
Zamarreño, Fernando
Costabel, Marcelo Daniel
García Zepeda, Eduardo
Salinas, Gustavo
Córsico, Betina
Ferreira, Ana María
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Cestode
Echinococcus
Hlbp
Lipoprotein
Antigen B
Tapeworm
topic Cestode
Echinococcus
Hlbp
Lipoprotein
Antigen B
Tapeworm
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Lipids are mainly solubilized by various families of lipid binding proteins which participate in their transport between tissues as well as cell compartments. Among these families, Hydrophobic Ligand Binding Proteins (HLBPs) deserve special consideration since they comprise intracellular and extracellular members, are able to bind a variety of fatty acids, retinoids and some sterols, and are present exclusively in cestodes. Since these parasites have lost catabolic and biosynthetic pathways for fatty acids and cholesterol, HLBPs are likely relevant for lipid uptake and transportation between parasite and host cells. Echinococcus granulosus antigen B (EgAgB) is a lipoprotein belonging to the HLBP family, which is very abundant in the larval stage of this parasite. Herein, we review the literature on EgAgB composition, structural organization and biological properties, and propose an integrated scenario in which this parasite HLBP contributes to adaptation to mammalian hosts by meeting both metabolic and immunomodulatory parasite demands.
Fil: Silva Alvarez, Maria Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Folle, Ana Maite. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Ramos, Ana Lía. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur; Argentina
Fil: García Zepeda, Eduardo. Universidad Nacional Autónoma de México; México
Fil: Salinas, Gustavo. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina
Fil: Ferreira, Ana María. Universidad del Uruguay. Facultad de Ciencias; Uruguay
description Lipids are mainly solubilized by various families of lipid binding proteins which participate in their transport between tissues as well as cell compartments. Among these families, Hydrophobic Ligand Binding Proteins (HLBPs) deserve special consideration since they comprise intracellular and extracellular members, are able to bind a variety of fatty acids, retinoids and some sterols, and are present exclusively in cestodes. Since these parasites have lost catabolic and biosynthetic pathways for fatty acids and cholesterol, HLBPs are likely relevant for lipid uptake and transportation between parasite and host cells. Echinococcus granulosus antigen B (EgAgB) is a lipoprotein belonging to the HLBP family, which is very abundant in the larval stage of this parasite. Herein, we review the literature on EgAgB composition, structural organization and biological properties, and propose an integrated scenario in which this parasite HLBP contributes to adaptation to mammalian hosts by meeting both metabolic and immunomodulatory parasite demands.
publishDate 2015
dc.date.none.fl_str_mv 2015-02
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/11336/39626
Silva Alvarez, Maria Valeria; Folle, Ana Maite; Ramos, Ana Lía; Zamarreño, Fernando; Costabel, Marcelo Daniel; et al.; Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface; Elsevier; Prostaglandins Leukotrienes and Essential Fatty Acids; 93; 2-2015; 17-23
0952-3278
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39626
identifier_str_mv Silva Alvarez, Maria Valeria; Folle, Ana Maite; Ramos, Ana Lía; Zamarreño, Fernando; Costabel, Marcelo Daniel; et al.; Echinococcus granulosus antigen B: A Hydrophobic Ligand Binding Protein at the host–parasite interface; Elsevier; Prostaglandins Leukotrienes and Essential Fatty Acids; 93; 2-2015; 17-23
0952-3278
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.plefa.com/article/S0952-3278(14)00152-5/fulltext
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plefa.2014.09.008
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0952327814001525
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 Elsevier
publisher.none.fl_str_mv Elsevier
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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