Abstract
Interferon-induced membrane protein 3 (IFITM3) is a key antiviral protein involved in the restriction of a number of viruses including influenza, dengue, ebola, and HIV. Despite its significance in the host innate immune response, very little is known about IFITM3's mechanism of action. Proteomic studies have determined IFITM3 is S-palmitoylated at multiple sites and this modification is necessary for its proper function. The S-palmitoylation of IFITM3 can change its subcellular localization; however, the effect it has on IFITM3 structure and function has not been characterized. An understanding of the structure, topology, and oligomeric state of lipidated IFITM3 would lead to a better understanding of its mechanism of action. To address these questions, we have optimized the expression, purification and site-specific lipidation of recombinant IFITM3 for in vitro reconstitution and structural studies. Through structural analysis and in vitro fusion studies, we may elucidate how this family of IFN-effectors prevents virus translocation across cellular membranes.
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