L. pneumophila is an environmental Gram-negative bacterium that survives in the environment by replicating within free-living amoebae. When transmitted to humans, it infects phagocytic immune cells within the lung, such as macrophages and monocytes, to cause disease. To survive and replicate within its hosts, Legionella uses a type-IVB secretion system to secrete >330 “effector” proteins into the host cell that manipulate various host processes to evade elimination by phago-lysosomal degradation and establish its intracellular replicative vacuole, the Legionella-containing vacuole (LCV). Legionella hijacks endoplasmic reticulum (ER) membranes to form the LCV and we hypothesise that it causes a loss of ER homeostasis, or ER stress, within the host cell.
The unfolded protein response (UPR) is a homeostatic response to ER stress but also plays an important role in infection and immunity. Legionella effectors have been previously shown to inhibit UPR signalling but whether the UPR restricts Legionella replication remains unknown. In this study, we have shown that pre-treatment of a human macrophage cell line with pharmacological inducers of ER stress, tunicamycin and thapsigargin, inhibits Legionella intracellular replication. Drug pre-treatment did not inhibit Legionella growth in vitro, phagocytic uptake of the bacterium or effector translocation via the type-IVB secretion system. Although tunicamycin was shown to enhance host apoptosis to inhibit bacterial replication, thapsigargin pre-treatment rather protected macrophages from Legionella-induced cytotoxicity. Together, these data suggest that ER stress restricts Legionella replication via a cell intrinsic mechanism, possibly a UPR-dependent mechanism, that is currently being investigated.
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