Here, an orthologue of far-6 in the model organism Caenorhabditis elegans ( Ce-far-6) was functionally characterised in a parasitic nematode, H. Localisation of the protein was shown in sections of paraffin-embedded worms after an immunohistochemistry (IHC) assay.
RNA interference (RNAi) and heterologous expression (rescuing) experiments were designed to explore the potential roles of the selected FAR protein in nematodes. Ligand binding assay and molecular docking were conducted to verify the fatty acid binding activities of FAR proteins of interest. Their transcription patterns in worms were also analysed to identify the targets. MethodsĪ genome-wide identification and curation were performed to screen the FAR family members of Haemonchus contortus. However, little is known about their detailed functional roles in either free-living or parasitic nematodes. Nematode-specific fatty acid- and retinol-binding protein (FAR) family is one approach that facilitates lipid acquisition, representing an Achilles heel and potential target against roundworms of socioeconomic significance. Nematodes have lost the ability to synthesise necessary lipids de novo and have complementally evolved the capacity to acquire fatty acids and their derivatives from a diet or host animal.
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