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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2014
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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. |
format | Online Article Text |
id | pubmed-4042634 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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