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Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition

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Siegrist, M. S., Unnikrishnan, Meera, McConnell, Matthew J., Borowsky, Mark, Cheng, T.-Y., Siddiqi, N., Fortune, S. M., Moody, D. Branch and Rubin, Eric J. (2009) Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition. Proceedings of the National Academy of Sciences of the United States of America, Volume 106 (Number 44). pp. 18792-18797. doi:10.1073/pnas.0900589106 ISSN 0027-8424.

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Official URL: http://dx.doi.org/10.1073/pnas.0900589106

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Abstract

The Esx secretion pathway is conserved across Gram-positive bacteria. Esx-1, the best-characterized system, is required for virulence of Mycobacterium tuberculosis, although its precise function during infection remains unclear. Esx-3, a paralogous system present in all mycobacterial species, is required for growth in vitro. Here, we demonstrate that mycobacteria lacking Esx-3 are defective in acquiring iron. To compete for the limited iron available in the host and the environment, these organisms use mycobactin, high-affinity iron-binding molecules. In the absence of Esx-3, mycobacteria synthesize mycobactin but are unable to use the bound iron and are impaired severely for growth during macrophage infection. Mycobacteria thus require a specialized secretion system for acquiring iron from siderophores.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Q Science > QR Microbiology
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Microbiology & Infection
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Secretion, Mycobacterium tuberculosis, Siderophores, Mycobacteria -- Metabolism, Iron -- Metabolism
Journal or Publication Title: Proceedings of the National Academy of Sciences of the United States of America
Publisher: National Academy of Sciences
ISSN: 0027-8424
Official Date: November 2009
Dates:
DateEvent
November 2009Published
Volume: Volume 106
Number: Number 44
Page Range: pp. 18792-18797
DOI: 10.1073/pnas.0900589106
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Burroughs Wellcome Fund (BWF), National Institutes of Health (U.S.) (NIH)
Grant number: R01 AI48704 and R0171155 (NIH)

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