A Proteomic View of Salmonella Typhimurium in Response to Phosphate Limitation

• Published in: Proteomes Vol. 6; no. 2; p. 19
• Main Authors: Jiang, Jiezhang, Yu, Kaiwen, Qi, Linlu, Liu, Yanhua, Cheng, Sen, Wu, Mei, Wang, Zhen, Fu, Jiaqi, Liu, Xiaoyun
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 25.04.2018; MDPI
• Subjects: Bacteria; Batch processes; Biodegradation; Deoxyribonucleic acid; DNA; E coli; Foodborne pathogens; Gene expression; Glycogen; Glycolysis; Homeostasis; Immunoblotting; Kinases; Labeling; Metabolism; N-Acetylglucosamine; Pathogens; Pentose phosphate pathway; Peptides; phosphate starvation; Phosphorus; Proteins; Salmonella; Salmonella Typhimurium; Signal transduction; the nag operon; the PhoR-PhoB two-component system; Trehalose; β-Galactosidase; Beijing China; United States > US; China; phosphate starvation; the PhoR-PhoB two-component system; Salmonella Typhimurium; the nag operon
• ISSN: 2227-7382; 2227-7382
• DOI: 10.3390/proteomes6020019

serovar Typhimurium ( Typhimurium), an important foodborne pathogen, often encounters phosphate (P ) shortage both in the environment and inside host cells. To gain a global view on its physiological responses to P starvation, we performed proteomic profiling of Typhimurium upon the shift from P -rich to P -low conditions. In addition to the Pho regulon, many metabolic processes were up-regulated, such as glycolysis, pentose phosphate pathway, pyrimidine degradation, glycogen, and trehalose metabolism, allowing us to chart an overview of Typhimurium carbon metabolism under P starvation. Furthermore, proteomic analysis of a mutant lacking (that encodes a key regulator of P shortage response) suggested that only a small subset of the altered proteins upon P limitation was PhoB-dependent. Importantly, we present evidence that Typhimurium -acetylglucosamine catabolism was induced under P -limiting conditions in a PhoB-dependent manner. Immunoblotting and β-galactosidase assays demonstrated that PhoB was required for the full activation of NagB, a key enzyme of this pathway, in response to low P . Thus, our study reveals that -acetylglucosamine catabolism may represent an additional PhoB-regulated pathway to tackle bacterial P shortage.