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| Nature. 2004 Nov 7 [Epub ahead of print] Links
Lipocalin 2 mediates an innate immune response to bacterial infection by
sequestrating iron.
Flo TH, Smith KD, Sato S, Rodriguez DJ, Holmes MA, Strong RK, Akira S, Aderem
A.
[1] Institute for Systems Biology, Seattle, Washington 98103, USA [2] Institute
for Cancer Research and Molecular Medicine, Norwegian university of Science and
Technology, 7489 Trondheim, Norway [3] These authors contributed equally to
this work.
Although iron is required to sustain life, its free concentration and
metabolism have to be tightly regulated. This is achieved through a variety of
iron-binding proteins including transferrin and ferritin. During infection,
bacteria acquire much of their iron from the host by synthesizing siderophores
that scavenge iron and transport it into the pathogen. We recently demonstrated
that enterochelin, a bacterial catecholate siderophore, binds to the host
protein lipocalin 2 (ref. 5). Here, we show that this event is pivotal in the
innate immune response to bacterial infection. Upon encountering invading
bacteria the Toll-like receptors on immune cells stimulate the transcription,
translation and secretion of lipocalin 2; secreted lipocalin 2 then limits
bacterial growth by sequestrating the iron-laden siderophore. Our finding
represents a new component of the innate immune system and the acute phase
response to infection.
PMID: 15531878 [PubMed - as supplied by publisher]
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