[Roles of bacterial and mammalian siderophores in host-pathogen interactions]

Iron is an essential nutriment for almost all forms of life, from bacteria to humans. Despite its key role in living organisms, iron becomes toxic at high concentrations. In the body, to circumvent this toxicity, almost all the intracellular iron is bound to proteins (especially to ferritin, a protein able to bind up to 4000 atoms of iron) and a small proportion (0.2% to 3%) to low molecular weight ligands (less than 2 kDa) constituting a free iron pool able to ensure the traffic of intracellular iron. A number of small molecules (citrate, phosphate, phospholipid, polypeptide) able to chelate iron, with variable affinities, have been known for a long time. In 2010, two teams have identified new mammal endogen chelators able to bind iron with similar chemical properties as bacterial siderophores. Recently, a few publications emphasized that most of the free iron present in the body cells is indeed linked to these siderophores, which play a key role in infected-host protection mechanisms during bacterial infections, through iron homeostasis and oxidative stress regulation.