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Iron metabolism at the host pathogen interface: lipocalin 2 and the pathogen-associated iroA gene cluster.
Title | Iron metabolism at the host pathogen interface: lipocalin 2 and the pathogen-associated iroA gene cluster. |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Smith, KD |
Journal | Int J Biochem Cell Biol |
Volume | 39 |
Issue | 10 |
Pagination | 1776-80 |
Date Published | 2007 |
ISSN | 1357-2725 |
Keywords | Acute-Phase Proteins, Animals, Bacterial Outer Membrane Proteins, Drug Design, Enterobactin, Gene Targeting, Glucosides, Host-Pathogen Interactions, Humans, Iron, Lipocalins, Models, Biological, Multigene Family, Proto-Oncogene Proteins |
Abstract | The host innate immune defense protein lipocalin 2 binds bacterial enterobactin siderophores to limit bacterial iron acquisition. To counteract this host defense mechanism bacteria have acquired the iroA gene cluster, which encodes enzymatic machinery and transporters that revitalize enterobactin in the form of salmochelin. The iroB enzyme introduces glucosyl residues at the C5 site on 2,3-dihydroxybenzoylserine moieties of enterobactin and thereby prevents lipocalin 2 binding. Additional strategies to evade lipocalin 2 have evolved in other bacteria, such as Mycobacteria tuberculosis and Bacillus anthracis. Targeting these specialized bacterial evasion strategy may provide a mechanism to reinvigorate lipocalin 2 in defense against specific pathogens. |
DOI | 10.1016/j.biocel.2007.07.003 |
Alternate Journal | Int. J. Biochem. Cell Biol. |
PubMed ID | 17714976 |