Synthetic porcine hepcidin exerts opposite roles in Escherichia coli and Salmonella infections [PublishAheadOfPrint]

Hepcidin, an antimicrobial peptide, was discovered to integrate diverse signals from iron status and infection threat and orchestrate a series of host protective responses. There have been several studies investigating the antimicrobial role of hepcidin but controversial. Here, we aim to examine the role of hepcidin in bacterial adherence and invasion in vitro. We found that porcine hepcidin could decrease the amount of extracellular pathogen enterotoxigenic Escherichia coli (ETEC) K88 that adhered to cells by aggregating bacteria. However, additing hepcidin to infected macrophages with intracellular pathogen Salmonella typhimurium enhanced the intracellular growth of pathogens by degradation of ferroportin, an iron export protein, and then sequestering intracellular iron. It was consisted with iron chelator deferiprone (DFO), which reduced intracellular bacterial growth. These results demonstrated hepcidin exhibited different functions on extracellular and intracellular bacterial infection, which suggested that different defense strateges should be taken to prevent bacterial infection.

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