The role of copper in the innate immune response to Salmonella enterica serovar Typhimurium
TL;DRAbstract
Salmonella enterica sv. Typhimurium (S. Typhimurium) causes gastroenteritis in humans and is used in the mouse as a model for human typhoid fever. It is an intracellular pathogen, which subverts normal phagolysosome formation to reside in specialized vesicles called Salmonella-containing vacuoles (SCV). Salmonella must acquire nutrients and defend against the antimicrobial action of the macrophage to survive in this intracellular environment. The importance of iron in Salmonella pathogenicity has long been recognized; in this study the role of copper in regulating Salmonella survival within macrophages was investigated. Infection of bone marrow-derived macrophages (BMM) with S. Typhimurium or treatment with LPS robustly increased the mRNA expression of genes encoding the copper transporters Ctr1, Ctr2 and Atp7a, divalent cation transporter Nramp1, copper chaperones Atox1, CCS and Cox17, as well as the multicopper ferroxidase Cp (ceruloplasmin), in both its secreted and anchored forms.
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Salmonella enterica sv. Typhimurium (S. Typhimurium) causes gastroenteritis in humans and is used in the mouse as a model for human typhoid fever. It is an intracellular pathogen, which subverts normal phagolysosome formation to reside in specialized vesicles called Salmonella-containing vacuoles (SCV). Salmonella must acquire nutrients and defend against the antimicrobial action of the macrophage to survive in this intracellular environment. The importance of iron in Salmonella pathogenicity has long been recognized; in this study the role of copper in regulating Salmonella survival within macrophages was investigated. Infection of bone marrow-derived macrophages (BMM) with S. Typhimurium or treatment with LPS robustly increased the mRNA expression of genes encoding the copper transporters Ctr1, Ctr2 and Atp7a, divalent cation transporter Nramp1, copper chaperones Atox1, CCS and Cox17, as well as the multicopper ferroxidase Cp (ceruloplasmin), in both its secreted and anchored forms.
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