In this study, we sought to implement a combined approach for comparative {Selleck Anti-infection Compound Library|Selleck Antiinfection Compound Library|Selleck Anti-infection Compound Library|Selleck Antiinfection Compound Library|Selleckchem Anti-infection Compound Library|Selleckchem Antiinfection Compound Library|Selleckchem Anti-infection Compound Library|Selleckchem Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|buy Anti-infection Compound Library|Anti-infection Compound Library ic50|Anti-infection Compound Library price|Anti-infection Compound Library cost|Anti-infection Compound Library solubility dmso|Anti-infection Compound Library purchase|Anti-infection Compound Library manufacturer|Anti-infection Compound Library research buy|Anti-infection Compound Library order|Anti-infection Compound Library mouse|Anti-infection Compound Library chemical structure|Anti-infection Compound Library mw|Anti-infection Compound Library molecular weight|Anti-infection Compound Library datasheet|Anti-infection Compound Library supplier|Anti-infection Compound Library in vitro|Anti-infection Compound Library cell line|Anti-infection Compound Library concentration|Anti-infection Compound Library nmr|Anti-infection Compound Library in vivo|Anti-infection Compound Library clinical trial|Anti-infection Compound Library cell assay|Anti-infection Compound Library screening|Anti-infection Compound Library high throughput|buy Antiinfection Compound Library|Antiinfection Compound Library ic50|Antiinfection Compound Library price|Antiinfection Compound Library cost|Antiinfection Compound Library solubility dmso|Antiinfection Compound Library purchase|Antiinfection Compound Library manufacturer|Antiinfection Compound Library research buy|Antiinfection Compound Library order|Antiinfection Compound Library chemical structure|Antiinfection Compound Library datasheet|Antiinfection Compound Library supplier|Antiinfection Compound Library in vitro|Antiinfection Compound Library cell line|Antiinfection Compound Library concentration|Antiinfection Compound Library clinical trial|Antiinfection Compound Library cell assay|Antiinfection Compound Library screening|Antiinfection Compound Library high throughput|Anti-infection Compound high throughput screening| Exoproteome analysis of different C. pseudotuberculosis strains. The strategy included: (i) the previously optimized TPP protocol for isolation of the extracellular proteins [11]; (ii) a newly introduced method of data-independent LC-MS acquisition (LC-MSE) for NVP-BSK805 protein identification and quantification [13, 14]; and (iii) the recently developed tool SurfG+ for in silico prediction of protein sub-cellular localization in Gram-positive bacteria [15]. We believe that the experimental approach used is very suitable for profiling bacterial exoproteomes,

as it shown to be easily applicable to different strains with very good reproducibility. This is an advantage over what is commonly observed for proteomic approaches based on two-dimensional (2D) gel electrophoresis, where there is more variability, but is apparently the method of choice for most of the bacterial exoproteome studies published recently [16–20]. Furthermore, the LC-MSE method provides high subproteome coverage, due to enhanced sensitivity, and allows for label-free analysis of differentially expressed proteins [14]; this latter

possibility enables the detection of variations FG-4592 mw in the exoproteomes of different strains that could be missed by simply profiling the exoproteins, and meets the growing interest in performing physiological proteomic studies of bacteria [21, 22]. We were able to identify 93 different C. pseudotuberculosis extracellular proteins

with high confidence by analyzing the exoproteomes of two strains isolated from different hosts that presented distinct virulence phenotypes under laboratory conditions [23, 24]. Most of the identified proteins were predicted in silico to ZD1839 chemical structure have an extracytoplasmic localization. To the best of our knowledge, these results compose the largest inventory of experimentally confirmed exoproteins of a single corynebacterial species to date. Importantly, the comparative exoproteome analyses permitted us to speculate on the probable contributions of different C. pseudotuberculosis extracellular proteins to the virulence of this bacterium. Results and Discussion Exoproteome analysis of Corynebacterium pseudotuberculosis The extracellular proteins of two C. pseudotuberculosis strains, one isolated from a goat (strain 1002) the other from a sheep (strain C231), cultivated in a chemically-defined medium, were extracted/concentrated by the TPP technique. The trypsinized protein samples were then submitted to LC-MSE analysis. Seventy soluble extracellular proteins of the 1002 strain could be confidentially identified by this methodology, whereas the number of proteins identified in the exoproteome of the C231 strain was sixty-seven. Altogether, 93 different C. pseudotuberculosis exoproteins were identified in this study (Figure 1).