Comparative investigation of lipid binding proteins of parasitic nematodes from the genus Trichinella
Final Report Abstract
Trichinellosis is a parasitic disease caused by nematodes of the genus Trichinella. Trichinella is often referred to as the largest intracellular parasite and invasion of vertebrate striated muscle cells by larvae is accompanied by dedifferentiation of the host myofiber into the nurse cell-parasite complex. Excretory-secretory proteins are involved in these processes. In our project we have identified and analysed a novel poly-cysteine and histidine-tailed metalloprotein (Ts-PCHTP) which is specific for Trichinelloidea, showing its potential as target for diagnostics and chemotherapy. The protein is mainly localized in the cuticle and other somatic tissues of the larvae, however, it is not excreted outside of the parasite. We propose a function in metal storage and/or transport. Since we ran into problems with our T. spiralis Lipid Binding Proteins (LBPs)-project, we turned to our model nematode Caenorhabditis elegans to investigate one of the fatty acid- and retinoid-binding protein family (FAR) members. Here, we were able to report the first high resolution x-ray crystallographic structure of a representative of the FAR family, the Ce-FAR-7, and also provide novel functional information on FAR proteins from nematodes.
Publications
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(2009). Fatty acid- and retinoid-binding proteins have distinct binding pockets for the two types of cargo. J Biol Chem. 284:35818-26
Jordanova R, Groves MR, Kostova E, Woltersdorf C, Liebau E, Tucker PA
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(2010). A novel secretory poly-cysteine and histidine-tailed metalloprotein (Ts-PCHTP) from Trichinella spiralis (Nematoda). PLoS One. 5:e13343
Radoslavov G, Jordanova R, Teofanova D, Georgieva K, Hristov P, Salomone-Stagni M, Liebau E, Bankov I
