Salmonella Typhimurium is a gastrointestinal pathogen that infects both humans and animals. S. Typhimurium infects epithelial cells and macrophages intracellularly, enabled by two specialised Type III Secretion Systems (T3SSs) which translocate effector proteins directly into the host cell cytosol. These effector proteins exert a range of pathogenic activities, including manipulation of innate immune signalling and programmed cell death processes. Our preliminary research shows that infection of immortalised murine macrophages with wild type S. Typhimurium induces the degradation of cellular inhibitor of apoptosis protein 1 (cIAP1), an important host cell adaptor of tumour necrosis factor receptor 1 (TNFR1) signalling and inhibitor of apoptotic cell death. Degradation of cIAP1 was associated with functional Salmonella Pathogenicity Island 1 (SPI-1) T3SS effector translocation, and was not prevented by pan-caspase, proteasomal or lysosomal inhibitors. Consistent with cIAP1-mediated inhibition of apoptosis, we observed strong association between loss of cIAP1 and increased cellular cytotoxicity. Anti-cIAP1 immunoblot detected a low molecular weight peptide following S. Typhimurium infection, suggesting that a SPI-1 effector may cleave cIAP1 during infection. Current work combines several molecular and in vitro techniques, aiming to elucidate the cIAP cleavage mechanism, and determine the responsible SPI-1 effector protein. Future work will assess the involvement of cIAP proteins in overall susceptibility to Salmonella infection in vivo. Together, these data provide early support for our hypothesis that cIAP1 depletion was induced by a S. Typhimurium SPI-1 effector in order to promote host cell death, and potentially dissemination of the bacterium.