Proteome profiling of Pseudomonas aeruginosa PAO1 identifies novel responders to copper stress

Bradley W. Wright, Karthik S. Kamath, Christoph Krisp, Mark P. Molloy*

*Corresponding author for this work

Research output: Contribution to journalArticle

3 Citations (Scopus)
8 Downloads (Pure)

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 languageEnglish
Article number69
Pages (from-to)1-13
Number of pages13
JournalBMC Microbiology
Volume19
DOIs
Publication statusPublished - 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

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