Identification of a secreted fatty acid and retinol-binding protein (Hp-FAR-1) from Heligmosomoides polygyrus

Bath, J.L. et al. (2009) Identification of a secreted fatty acid and retinol-binding protein (Hp-FAR-1) from Heligmosomoides polygyrus. Journal of Nematology, 41(3), pp. 228-233.

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Hp-FAR-1 is a major, secreted antigen of the parasitic nematode Heligmosomoides polygyrus, a laboratory mouse model frequently used to study the cellular mechanisms of chronic helminth infections. The DNA encoding Hp-FAR-1 was recovered by screening a fourth larval (L-4) H. polygyrus DNA expression library, using antibodies raised against L-4 stage excretory/secretory (E/S) proteins. Predictions of secondary structure based on the Hp-FAR-1 amino acid sequence indicated that an alpha-helix predominates in Hp-FAR-1, possibly with some coiled-coil conformation, with to beta-structure. Fluorescence-based ligand binding analysis confirmed that the recombinant Hp-FAR-1 (rHp-FAR-1) binds the fluorescent fatty acid analog 11-((5-[dimethylaminoaphthalene-1-sulfonyl)amino)undecanoic acid (DAUDA), and by competition oleic acid. RT-PCR amplification of the hp-far-1 gene indicated that the gene is transcribed in all parasitic stages of the organism's life cycle. The presence of a secreted FAR protein in the well-defined laboratory model of H. polygyrus provides an excellent model for the further study and analysis of the in vivo role of secreted FAR proteins in parasitism, and supports the mounting evidence that secreted FAR proteins play a major role in nematode parasitism

Item Type:Articles
Glasgow Author(s) Enlighten ID:Kennedy, Professor Malcolm
Authors: Bath, J.L., Robinson, M., Kennedy, M., Agbasi, C., Linz, L., Maetzold, E., Scheidt, M., Knox, M., Ram, D., Hein, J., Clark, C., and Drees, J.
College/School:College of Medical Veterinary and Life Sciences > School of Life Sciences
Journal Name:Journal of Nematology

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