Nanoparticle formulation for the development of a dog nanovaccine against Cystic Echinococcosis.

Cystic Echinococcosis is a cosmopolitan zoonosis closely linked to poverty and ignorance. It affects both cattle and humans, causing significant losses to both human and animal health. To date, there is no effective way to combat this.

Dimerization, host-parasite communication and expression studies of an Echinococcus granulosus 2DBD nuclear receptor.

Nuclear receptors (NRs) are ligand-modulated transcription factors that regulate various biological processes, such as metabolism, development and reproduction. Although NRs with two DNA-binding domains (2DBD) were identified in Schistosoma mansoni (Platyhelminth, Trematoda) more than fifteen years ago, these proteins have been poorly studied. 2DBD-NRs could become attractive therapeutic targets to combat parasitic diseases such as cystic echinococcosis since this type of protein is absent in vertebrate hosts.

Echinococcus granulosus fatty acid binding proteins subcellular localization.

Two fatty acid binding proteins, EgFABP1 and EgFABP2, were isolated from the parasitic platyhelminth Echinococcus granulosus. These proteins bind fatty acids and have particular relevance in flatworms since de novo fatty acids synthesis is absent. Therefore platyhelminthes depend on the capture and intracellular distribution of host's lipids and fatty acid binding proteins could participate in lipid distribution.

Towards an understanding of Mesocestoides vogae fatty acid binding proteins' roles.

Two fatty acid binding proteins, MvFABPa and MvFABPb were identified in the parasite Mesocestoides vogae (Platyhelmithes, Cestoda). Fatty acid binding proteins are small intracellular proteins whose members exhibit great diversity. Proteins of this family have been identified in many organisms, of which Platyhelminthes are among the most primitive.

Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.

Background: Growth and maintenance of hydatid cysts produced by Echinococcus granulosus have a high requirement for host lipids for biosynthetic processes, membrane building and possibly cellular and developmental signalling. This requires a high degree of lipid trafficking facilitated by lipid transporter proteins. Members of the fatty acid binding protein (FABP) family have been identified in Echinococcus granulosus, one of which, EgFABP1 is expressed at the tegumental level in the protoscoleces, but it has also been described in both hydatid cyst fluid and secretions of protoscoleces.

Lipid binding proteins from parasitic platyhelminthes.

TWO MAIN FAMILIES OF LIPID BINDING PROTEINS HAVE BEEN IDENTIFIED IN PARASITIC PLATYHELMINTHES: hydrophobic ligand binding proteins (HLBPs) and fatty acid binding proteins (FABPs). Members of the former family of proteins are specific to the Cestoda class, while FABPs are conserved across a wide range of animal species. Because Platyhelminthes are unable to synthesize their own lipids, these lipid-binding proteins are important molecules in these organisms.

Echinococcus granulosus tropomyosin isoforms: from gene structure to expression analysis.

Tropomyosins (Trps) constitute a family of actin filament-binding proteins found in all eukaryotic cells. In muscle cells, they play a central role in contraction by regulating calcium-sensitive interaction of actin and myosin. In non-muscle cells, tropomyosins regulate actin filament organization and dynamics.

An oral recombinant vaccine in dogs against Echinococcus granulosus, the causative agent of human hydatid disease: a pilot study.

Dogs are the main source of human cystic echinococcosis. An oral vaccine would be an important contribution to control programs in endemic countries. We conducted two parallel experimental trials in Morocco and Tunisia of a new oral vaccine candidate against Echinococcus granulosus in 28 dogs.

Two novel Mesocestoides vogae fatty acid binding proteins--functional and evolutionary implications.

This work describes two new fatty acid binding proteins (FABPs) identified in the parasite platyhelminth Mesocestoides vogae (syn. corti). The corresponding polypeptide chains share 62% identical residues and overall 90% similarity according to CLUSTALX default conditions.

The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1.

We describe the 1.6 A crystal structure of the fatty-acid-binding protein EgFABP1 from the parasitic platyhelminth Echinococcus granulosus. E.