The bacterial pathogen, Legionella pneumphila (Lp) has evolved to replicate within aquatic protozoa and mammalian macrophages and has emerged as the causative agent of a life-threatening lung infection, Legionnaire’s Disease. Infection commences with the inhalation of contaminated aerosols and the uptake of Lp by alveolar macrophages. Within macrophages Lp evades destruction by replicating within a “Legionella-containing vacuole” (LCV). LCV biogenesis depends on the secretion of more than 300 virulence (effector) proteins via the Dot/Icm secretion system. Many effectors share similarity with eukaryotic proteins and hijack host processes through molecular mimicry. These eukaryotic-like effectors are believed to be acquired by inter-kingdom RNA transfer via an unknown mechanism. In this study, we investigated the impact of Lp effectors on host nuclear function. We hypothesized that nuclear localized effectors subvert the host transcriptional response to infection and/or play a role in acquisition of eukaryotic genetic material. We performed a pilot study in which human macrophages were infected with wild type or ΔdotA mutant Lp, nuclear fractions were enriched and analysed by mass-spectrometry. We identified several effectors that associate with host nuclear components, including effectors SnpL and NupT. We observed that SnpL traffics to the host cell nucleus and binds to host transcription elongation factor, SUPT5H. Macrophages expressing SnpL showed widespread upregulation of host transcription, suggesting that the binding of SnpL to SUPT5H disrupts the transcriptional pausing activity of the DSIF complex. In contrast to SnpL, NupT localised predominantly onto the LCV membrane. NupT, along with the Dot/Icm effectors, Lem22 and LegC6, share structural similarity with host nucleoporin proteins (NUPs) from the nuclear pore complex. Preliminary BirA biotin ligase experiments suggested these effectors come into close proximity with several host NUPs, that have been associated with the LCV through proteomics studies. We hypothesize these effectors, together with recruited host proteins, form a nuclear pore-like complex in the LCV, which may be a potential mechanism by which eukaryotic RNA is transported into the LCV.