Abstract
Background: The opportunistic pathogen, Pseudomonas aeruginosa is well known for its environmental and metabolic versatility, yet many of the functions of its gene-products remain to be fully elucidated. This study's objective was to illuminate the potential functions of under-described gene-products during the medically relevant copper-stress condition.
Results: We used data-independent acquisition mass spectrometry to quantitate protein expression changes associated with copper stress in P. aeruginosa PAO1. Approximately 2000 non-redundant proteins were quantified, with 78 proteins altering in abundance by +/- 1.5-fold or more when cultured to mid-log growth in the presence of 50 μM copper sulfate. One-third of those differentially expressed proteins have no prior established functional roles.
Conclusions: This study provides evidence for the functional involvement of some specific proteins in enabling P. aeruginosa to survive under sub-lethal concentrations of copper. This further paves the way for targeted investigations into the specific mechanisms of their activity.
Original language | English |
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Article number | 69 |
Pages (from-to) | 1-13 |
Number of pages | 13 |
Journal | BMC Microbiology |
Volume | 19 |
DOIs | |
Publication status | Published - 1 Apr 2019 |
Bibliographical note
Copyright the Author(s) 2019. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.Keywords
- Mass spectrometry
- Copper stress
- Proteome
- Pseudomonas aeruginosa