Echinococcus granulosus antigen B: a hydrophobic ligand binding protein at the host-parasite interface.

SILVA V; FOLLE AM; RAMOS AL; ZAMARREÑO, F.; COSTABEL MD; GARCÍA-ZEPEDA E; SALINAS G; CÓRSICO B; FERREIRA AM

PROSTAGLANDINS LEUKOTRIENES AND ESSENTIAL FATTY ACIDS

ELSEVIER SCI LTD

Lugar: Amsterdam; Año: 2014

0952-3278

Physiological lipids are mainly solubilised 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 degrading 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 a novel scenario in which this parasite HLBP contributes to adaptation to mammalian hosts by meeting both metabolic and immunomodulatory parasite demands.