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Abstract
First identified as a neutrophil granule component, neutrophil gelatinase-associated
lipocalin (NGAL; also called human neutrophil lipocalin, 24p3, uterocalin, or neu-related
lipocalin) is a member of the lipocalin family of binding proteins. Putative NGAL
ligands, including neutrophil chemotactic agents such as N-formylated tripeptides,
have all been refuted by recent biochemical and structural results. NGAL has subsequently
been implicated in diverse cellular processes, but without a characterized ligand,
the molecular basis of these functions remained mysterious. Here we report that NGAL
tightly binds bacterial catecholate-type ferric siderophores through a cyclically
permuted, hybrid electrostatic/cation-pi interaction and is a potent bacteriostatic
agent in iron-limiting conditions. We therefore propose that NGAL participates in
the antibacterial iron depletion strategy of the innate immune system.