Characterisation of the Native Lipid Moiety of Echinococcus granulosus Antigen B

Dublin Core

Título

Characterisation of the Native Lipid Moiety of Echinococcus granulosus Antigen B

Tema

ECHINOCOCCUS GRANULOSUS
BIOQUÍMICA
LÍPIDOS
ANTÍGENOS
ENFERMEDADES PARASITARIAS
BIBLIOGRAFÍA NACIONAL QUÍMICA
2012

Abstract

Antigen B (EgAgB) is the most abundant and immunogenic antigen produced by the larval stage (metacestode) of Echinococcus granulosus. It is a lipoprotein, the structure and function of which have not been completely elucidated. EgAgB apolipoprotein components have been well characterised; they share homology with a group of hydrophobic ligand binding proteins (HLBPs) present exclusively in cestode organisms, and consist of different isoforms of 8-kDa proteins encoded by a polymorphic multigene family comprising five subfamilies (EgAgB1 to EgAgB5). In vitro studies have shown that EgAgB apolipoproteins are capable of binding fatty acids. However, the identity of the native lipid components of EgAgB remains unknown. The present work was aimed at characterising the lipid ligands bound to EgAgB in vivo. EgAgB was purified to homogeneity from hydatid cyst fluid and its lipid fraction was extracted using chloroform:methanol mixtures. This fraction constituted approximately 40–50% of EgAgB total mass. High-performance thin layer chromatography revealed that the native lipid moiety of EgAgB consists of a variety of neutral (mainly triacylglycerides, sterols and sterol esters) and polar (mainly phosphatidylcholine) lipids. Gas-liquid chromatography analysis showed that 16:0, 18:0 and 18:1(n-9) are the most abundant fatty acids in EgAgB. Furthermore, size exclusion chromatography coupled to light scattering demonstrated that EgAgB comprises a population of particles heterogeneous in size, with an average molecular mass of 229 kDa. Our results provide the first direct evidence of the nature of the hydrophobic ligands bound to EgAgB in vivo and indicate that the structure and composition of EgAgB lipoprotein particles are more complex than previously thought, resembling high density plasma lipoproteins. Results are discussed considering what is known on lipid metabolism in cestodes, and taken into account the Echinococcus spp. genomic information regarding both lipid metabolism and the EgAgB gene family.

Autor

Obal, Gonzalo
Ramos, Ana Lía
Silva, Valeria
Lima, Analía
Batthyany, Carlos
Bessio, María Inés
Ferreira, Ana María

Fuente

PloS Neglected Tropical Diseases v. 6, no. 5, 2012. -- e.1642

Editor

Dalton, John Pius McGill University, Canada

Fecha

2012

Derechos

La legislación uruguaya protege el derecho de autor sobre toda creación literaria, científica o artística, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeción a lo establecido por el derecho común y las siguientes leyes
(LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)
ADVERTENCIA - La consulta de este documento queda condicionada a la aceptación de las siguientes condiciones de uso: Este documento es únicamente para usos privados enmarcados en actividades de investigación y docencia. No se autoriza su reproducción con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilización o cita de partes debe indicarse el nombre de la persona autora.

Formato

PDF

Idioma

Inglés

Tipo

Artículo

Identificador

ISSN 1935-2727

Document Item Type Metadata

Original Format

PDF
Fecha de agregación
July 27, 2012
Colección
Bibliografía Nacional Química
Tipo de Elemento
Document
Etiquetas
, , ,
Citación
Obal, Gonzalo, “Characterisation of the Native Lipid Moiety of Echinococcus granulosus Antigen B,” RIQUIM - Repositorio Institucional de la Facultad de Química - UdelaR, accessed October 21, 2017, http://riquim.fq.edu.uy/items/show/5.
Archivos