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Lookup NU author(s): Dr Emma Tarrant, Jack Stevenson, Dr Anna Barwinska-SendraORCiD, Louisa Stewart, Dr Kevin WaldronORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Copper toxicity has been a long-term selection pressure on bacteria due to its presence in the environment and its use as an antimicrobial agent by grazing protozoa, by phagocytic cells of the immune system, and in man-made medical and commercial products. There is recent evidence that exposure to increased copper stress may have been a key driver in the evolution and spread of methicillin-resistant Staphylococcus aureus, a globally important pathogen that causes significant mortality and morbidity worldwide. Yet it is unclear how S. aureus physiology is affected by copper stress or how it adapts in order to be able to grow in the presence of excess copper. Here, we have determined quantitatively how S. aureus alters its proteome during growth under copper stress conditions, comparing this adaptive response in two different types of growth regime. We found that the adaptive response involves induction of the conserved copper detoxification system as well as induction of enzymes of central carbon metabolism, with only limited induction of proteins involved in the oxidative stress response. Further, we identified a protein that binds copper inside S. aureus cells when stressed by copper excess. This copper-binding enzyme, a glyceraldehyde-3-phosphate dehydrogenase essential for glycolysis, is inhibited by copper in vitro and inside S. aureus cells. Together, our data demonstrate that copper stress leads to the inhibition of glycolysis in S. aureus, and that the bacterium adapts to this stress by altering its central carbon utilisation pathways
Author(s): Tarrant E, Riboldi GP, McIlvin MR, Stevenson J, Barwinska-Sendra A, Stewart LJ, Saitob MA, Waldron KJ
Publication type: Article
Publication status: Published
Journal: Metallomics
Year: 2019
Volume: 11
Issue: 1
Pages: 183-200
Print publication date: 01/01/2019
Online publication date: 16/11/2018
Acceptance date: 19/10/2018
Date deposited: 20/12/2018
ISSN (print): 1756-5901
ISSN (electronic): 1756-591X
Publisher: Royal Society of Chemistry
URL: https://doi.org/10.1039/C8MT00239H
DOI: 10.1039/C8MT00239H
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