Proteomics insights into the Burkholderia cenocepacia phosphorus stress response |
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Authors: | Holly Shropshire Rebekah A. Jones María M. Aguilo-Ferretjans David J. Scanlan Yin Chen |
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Affiliation: | 1. BBSRC Midlands Integrative Biosciences Training Partnership, University of Warwick, Coventry, CV4 7AL UK School of Life Sciences, University of Warwick, Coventry, CV4 7AL UK;2. School of Life Sciences, University of Warwick, Coventry, CV4 7AL UK |
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Abstract: | The Burkholderia cepacia complex is a group of Burkholderia species that are opportunistic pathogens causing high mortality rates in patients with cystic fibrosis. An environmental stress often encountered by these soil-dwelling and pathogenic bacteria is phosphorus limitation, an essential element for cellular processes. Here, we describe cellular and extracellular proteins differentially regulated between phosphate-deplete (0 mM, no added phosphate) and phosphate-replete (1 mM) growth conditions using a comparative proteomics (LC–MS/MS) approach. We observed a total of 128 and 65 unique proteins were downregulated and upregulated respectively, in the B. cenocepacia proteome. Of those downregulated proteins, many have functions in amino acid transport/metabolism. We have identified 24 upregulated proteins that are directly/indirectly involved in inorganic phosphate or organic phosphorus acquisition. Also, proteins involved in virulence and antimicrobial resistance were differentially regulated, suggesting B. cenocepacia experiences a dramatic shift in metabolism under these stress conditions. Overall, this study provides a baseline for further research into the biology of Burkholderia in response to phosphorus stress. |
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