Proteomics insights into the Burkholderia cenocepacia phosphorus stress response

Abstract

Summary 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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