Echinococcus granulosus antigen B: a Hydrophobic Ligand Binding Protein at the host-parasite interface

Prostaglandins Leukot Essent Fatty Acids. 2015 Feb:93:17-23. doi: 10.1016/j.plefa.2014.09.008. Epub 2014 Oct 7.

Abstract

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.

Keywords: Antigen B; Cestode; Echinococcus; HLBP; Lipoprotein; Tapeworm.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / metabolism
  • Echinococcosis / parasitology
  • Echinococcus granulosus / growth & development
  • Echinococcus granulosus / physiology*
  • Host-Parasite Interactions*
  • Humans
  • Lipoproteins / chemistry
  • Lipoproteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Sequence Alignment

Substances

  • Carrier Proteins
  • Lipoproteins
  • antigen B, Echinococcus granulosus