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Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron

Author

Listed:
  • Trude H. Flo

    (Institute for Systems Biology
    Norwegian University of Science and Technology)

  • Kelly D. Smith

    (Institute for Systems Biology
    University of Washington)

  • Shintaro Sato

    (Osaka University, and Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation)

  • David J. Rodriguez

    (Institute for Systems Biology)

  • Margaret A. Holmes

    (Fred Hutchinson Cancer Research Center)

  • Roland K. Strong

    (Fred Hutchinson Cancer Research Center)

  • Shizuo Akira

    (Osaka University, and Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation)

  • Alan Aderem

    (Institute for Systems Biology)

Abstract

Although iron is required to sustain life, its free concentration and metabolism have to be tightly regulated1. This is achieved through a variety of iron-binding proteins including transferrin and ferritin2. During infection, bacteria acquire much of their iron from the host by synthesizing siderophores that scavenge iron and transport it into the pathogen3,4. 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.

Suggested Citation

  • Trude H. Flo & Kelly D. Smith & Shintaro Sato & David J. Rodriguez & Margaret A. Holmes & Roland K. Strong & Shizuo Akira & Alan Aderem, 2004. "Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron," Nature, Nature, vol. 432(7019), pages 917-921, December.
    • Handle: RePEc:nat:nature:v:432:y:2004:i:7019:d:10.1038_nature03104
    DOI: 10.1038/nature03104
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