Siderophores are essential factors for iron (Fe) acquisition in bacteria during colonization
and infection of eukaryotic hosts, which restrain iron access through iron-binding protein …

Salmochelins represent novel carbohydrate containing catecholate siderophores, which are
excreted by Salmonella enterica and uropathogenic Escherichia coli strains under low-iron …

The lipocalins are secreted proteins that bind small organic molecules. Scn-Ngal (also
known as neutrophil gelatinase associated lipocalin, siderocalin, lipocalin 2) sequesters …

To acquire essential Fe (III), bacteria produce and secrete siderophores with high affinity
and selectivity for Fe (III) to mediate its uptake into the cell. Here, we show that the …

Microorganisms produce siderophores to facilitate iron uptake and even though this trait has
been extensively studied, there is growing evidence suggesting that siderophores may have …

Iron is necessary for the survival of almost all aerobic organisms. In the mammalian host,
iron is a required cofactor for the assembly of functional iron-sulfur (Fe-S) cluster proteins …

In response to microbial infection, expression of the defensin-like peptide hepcidin (encoded
by Hamp) is induced in hepatocytes to decrease iron release from macrophages. To …

The siderophore salmochelin is produced under iron-poor conditions by Salmonella and
many uropathogenic Escherichia coli strains. The production of salmochelin, a C …

Producing novel enzymes that are catalytically active in vitro and biologically functional in
vivo is a key goal of synthetic biology. Here we describe Syn-F4, the first de novo protein that …

Numerous pathogenic microorganisms secrete small molecule chelators called
siderophores defined by their ability to bind extracellular ferric iron, making it bioavailable to …