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Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection

Competition for iron influences host–pathogen interactions. Pathogens secrete small iron-binding moieties, siderophores, to acquire host iron. In response, the host secretes siderophore-binding proteins, such as lipocalin 24p3, which limit siderophore-mediated iron import into bacteria. Mammals prod...

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Autores principales: Liu, Zhuoming, Reba, Scott, Chen, Wei-Dong, Porwal, Suheel Kumar, Boom, W. Henry, Petersen, Robert B., Rojas, Roxana, Viswanathan, Rajesh, Devireddy, L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4042634/
https://www.ncbi.nlm.nih.gov/pubmed/24863067
http://dx.doi.org/10.1084/jem.20132629
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author Liu, Zhuoming
Reba, Scott
Chen, Wei-Dong
Porwal, Suheel Kumar
Boom, W. Henry
Petersen, Robert B.
Rojas, Roxana
Viswanathan, Rajesh
Devireddy, L.
author_facet Liu, Zhuoming
Reba, Scott
Chen, Wei-Dong
Porwal, Suheel Kumar
Boom, W. Henry
Petersen, Robert B.
Rojas, Roxana
Viswanathan, Rajesh
Devireddy, L.
author_sort Liu, Zhuoming
collection PubMed
description Competition for iron influences host–pathogen interactions. Pathogens secrete small iron-binding moieties, siderophores, to acquire host iron. In response, the host secretes siderophore-binding proteins, such as lipocalin 24p3, which limit siderophore-mediated iron import into bacteria. Mammals produce 2,5-dihydroxy benzoic acid, a compound that resembles a bacterial siderophore. Our data suggest that bacteria use both mammalian and bacterial siderophores. In support of this idea, supplementation with mammalian siderophore enhances bacterial growth in vitro. In addition, mice lacking the mammalian siderophore resist E. coli infection. Finally, we show that the host responds to infection by suppressing siderophore synthesis while up-regulating lipocalin 24p3 expression via TLR signaling. Thus, reciprocal regulation of 24p3 and mammalian siderophore is a protective mechanism limiting microbial access to iron.
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spelling pubmed-40426342014-12-02 Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection Liu, Zhuoming Reba, Scott Chen, Wei-Dong Porwal, Suheel Kumar Boom, W. Henry Petersen, Robert B. Rojas, Roxana Viswanathan, Rajesh Devireddy, L. J Exp Med Article Competition for iron influences host–pathogen interactions. Pathogens secrete small iron-binding moieties, siderophores, to acquire host iron. In response, the host secretes siderophore-binding proteins, such as lipocalin 24p3, which limit siderophore-mediated iron import into bacteria. Mammals produce 2,5-dihydroxy benzoic acid, a compound that resembles a bacterial siderophore. Our data suggest that bacteria use both mammalian and bacterial siderophores. In support of this idea, supplementation with mammalian siderophore enhances bacterial growth in vitro. In addition, mice lacking the mammalian siderophore resist E. coli infection. Finally, we show that the host responds to infection by suppressing siderophore synthesis while up-regulating lipocalin 24p3 expression via TLR signaling. Thus, reciprocal regulation of 24p3 and mammalian siderophore is a protective mechanism limiting microbial access to iron. The Rockefeller University Press 2014-06-02 /pmc/articles/PMC4042634/ /pubmed/24863067 http://dx.doi.org/10.1084/jem.20132629 Text en © 2014 Liu et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Article
Liu, Zhuoming
Reba, Scott
Chen, Wei-Dong
Porwal, Suheel Kumar
Boom, W. Henry
Petersen, Robert B.
Rojas, Roxana
Viswanathan, Rajesh
Devireddy, L.
Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
title Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
title_full Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
title_fullStr Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
title_full_unstemmed Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
title_short Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
title_sort regulation of mammalian siderophore 2,5-dhba in the innate immune response to infection
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4042634/
https://www.ncbi.nlm.nih.gov/pubmed/24863067
http://dx.doi.org/10.1084/jem.20132629
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