The siderophore enterobactin (Ent) is produced by enteric bacteria to mediate iron uptake.
Ent scavenges iron and is taken up by the bacteria as the highly stable ferric complex [FeIII …

Iron is required for virulence of most bacterial pathogens, many of which rely on
siderophores, small-molecule chelators, to scavenge iron in mammalian hosts. As an …

Both host and pathogen competitively manipulate coordination environments during
bacterial infections. Human cells release the innate immune protein siderocalin (Scn, also …

Bacteria have aggressive acquisition processes for iron, an essential nutrient. Siderophores
are small iron chelators that facilitate cellular iron transport. The siderophore enterobactin is …

The mammalian protein siderocalin binds and inactivates the ferric complex of the bacterial
siderophore enterobactin with a K d value similar to that of the bacterial receptor FepA …

The human protein siderocalin (Scn) inhibits bacterial iron acquisition by binding catechol
siderophores. Several pathogenic bacteria respond by making stealth siderophores that are …

Many bacteria, including numerous human pathogens, synthesize small molecules known
as siderophores to scavenge iron. Enterobactin, a siderophore produced by enteric bacteria …

Bacteria use tight-binding, ferric-specific chelators called siderophores to acquire iron from
the environment and from the host during infection; animals use proteins such as transferrin …

Siderocalin, a member of the lipocalin family of binding proteins, is found in neutrophil
granules, uterine secretions, and at markedly elevated levels in serum and synovium during …

Iron is essential for the survival of almost all bacteria. Vibrio cholerae acquires iron through
the secretion of a catecholate siderophore called vibriobactin. At present, how vibriobactin …