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Targeting parasite FAR proteins in an attempt to restore host mucosal immunity during helminth infections

Hp‐FAR‐1 is a fatty acid and retinol binding protein that is secreted by the mouse parasite H. polygyrus. Previous groups in our lab have identified that the protein is secreted during each of the stages of the parasite's lifecycle. The corresponding gene, hp‐far‐1 was cloned into the pET‐30a vector and the expressed recombinant protein was purified on a HIS‐trap column and eluted in 500mM imidazole buffer. We demonstrate the binding capabilities and dissociation constants for both fatty acids and retinol with the purified recombinant protein. Hp‐FAR‐1's ability to bind retinol is of particular interest, given that retinol is the ligand for the retinoid X receptor, the transcriptional factor which controls the gene encoding IL‐4. IL‐4 deficiency has been demonstrated to contribute greatly to the severity of helminth infections. We are currently studying the effects of oral all trans‐retinoic acid (ATRA) treatment on H. polygyrus infected Balb/c mice. We hypothesize that treatment with ATRA will decrease the localized Th2 cell polarization, decrease parasitic worm burdens, and possibly (by preventing immunosuppression) correlate with improved immunity to protect against reinfection.