Article ID Journal Published Year Pages File Type
4370942 Experimental Parasitology 2016 4 Pages PDF
Abstract

•Echinococcus granulosus FABPs subcellular localization was analyzed by 2D-PAGE, WB and MS.•Cytosolic, nuclear, mitochondrial and microsomal larvae fractions were purified.•Three EgFABP1 isoforms were identified in each fraction.•Probably EgFABP2 protein expression is low or absent in protoscoleces.•EgFABP1 isoforms could be involved in several cellular processes.

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. To elucidate EgFABP's roles, we investigated their intracellular distribution in the larval stage by a proteomic approach. Our results demonstrated the presence of EgFABP1 isoforms in cytosolic, nuclear, mitochondrial and microsomal fractions, suggesting that these molecules could be involved in several cellular processes.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide

Related Topics
Life Sciences Immunology and Microbiology Parasitology
Authors
, ,