Rabies is a zoonotic disease caused by lyssaviruses, which has a nearly 100% case-fatality rate resulting in 60,000 human deaths yearly. Bats are an important reservoir for lyssaviruses, throughout the world and in Australia, and different bat species harbor different lyssavirus strains such as the Australian Bat Lyssavirus (ABLV) from frugivorous bats and ABLV from insectivorous bats, which differ in their phenotype in vitro. Central to the pathogenesis of lyssaviruses is their capacity to remain largely ‘invisible’ to the immune system through their ability to inhibit with high specificity the interferon (IFN)-dependent innate immune response, the first line of defence against viruses. This depends on the viral phosphoprotein (P), which is able to block both IFN induction in response to infection, and signalling by IFN cytokines, thereby preventing the expression of antiviral IFN-stimulated genes (ISG). Although the ability of P protein to bind to STAT transcription factors is well established, and is known to be critical to disease in laboratory animals, the precise mechanisms by which P modulates STAT functions remain largely unresolved. In particular, P protein is known to undergo import to the host cell nucleus via a complex array of interactions with nuclear transport machinery, and is expressed as multiple isoforms with diverse nuclear import activities, but the roles of this activity in modulating ISG expression is unresolved. Using comparative analysis of a prototype rabies virus strain and two strains of the closely related ABLV, that differ in these functions, we are investigating the molecular basis and functional outcomes of nuclear import in viral immune evasion, and the impact of nuclear localization on ISG expression. This study should expend our understanding of IFN signalling inhibition and offer new avenues for antiviral drug development. This is also the first comparative analysis of two ABLV strains from different bat species.