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. Author manuscript; available in PMC: 2015 Nov 1.
Published in final edited form as: FEMS Microbiol Rev. 2014 Sep 29;38(6):1235–1249. doi: 10.1111/1574-6976.12087

Figure 1. Fe limitation by the host.

Figure 1

In erythrocytes, Fe is complexed within heme and bound by hemoglobin. Upon erythrocyte lysis, hemoglobin is scavenged by haptoglobin and the complex is recognized by CD163 on macrophages, heme is bound by hemopexin, and free Fe is foraged by transferrin and lactoferrin, which is present in the secondary granules of neutrophils. Neutrophils also release siderocalin which complexes with mammalian and bacterial siderophores. Intracellular Fe stores are maintained in association with ferritin.