the IMPa is prevented from playing its normal role in mediating nuclear import of the STAT (signal transducer and activator of transcription) proteins in response to interferon (IFN), as part of the innate immune response (see [59]). Thus, it seems that various cytoplasmically replicating RNA viruses disrupt the cellular nuclear transport machinery in order to subvert the host cell transport processes necessary for the anti-viral response.

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Ivermectin's broad spectrum antiviral activity relates to its ability to target the host importin (IMP) a/ß1 nuclear transport proteins responsible for nuclear entry of cargoes such as integrase and NS5. We establish for the first time that ivermectin can dissociate the preformed IMPa/ß1 heterodimer, as well as prevent its formation, through binding to the IMPa armadillo (ARM) repeat domain to impact IMPa thermal stability and a-helicity. We show that ivermectin inhibits NS5-IMPa interaction in a cell context using quantitative bimolecular fluorescence complementation.

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