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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/39626
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
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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 Técnicas2025-09-29T09:56:56Zoai: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:34982025-09-29 09:56:56.362CONICET 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 |
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CONICET Digital (CONICET) |
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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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score |
13.070432 |