maculans isolate silenced in cpcA. RJ quantified sirodesmin PL. BJH conceived the study, and drafted the manuscript. All authors read and approved the final manuscript.”
“Background Campylobacter jejuni is a human pathogen and the leading cause of acute bacterial gastroenteritis. As a commensal organism for many warm-blooded animals, especially in the gastrointestinal tract of poultry, C jejuni is also isolated from a wide variety of watery environmental sources [1, 2]. Thus, the ability of C. jejuni

to sense and respond to diverse environmental stimuli and to adapt gene expression Vorinostat to changes in external conditions is crucial for its pathogenesis, commensalism and survival outside the host organism. Recent experiments have revealed many changes in the C. jejuni transcriptome and proteome that are driven by environmental stimuli. These include AP26113 solubility dmso temperature, oxygen tension, iron concentration, sodium deoxycholate concentration and pH of the culture medium [3–7]. C. jejuni’s

phase of life – planktonic vs biofilm – also shows a great difference in the microorganism’s protein profile [8, 9]. Campylobacter gene expression is coupled to environmental cues mostly by two-component signal transduction systems (TCSTS) [10–14]. The activity and the amount of a specific protein can also be affected by posttranslational modifications such as glycosylation, proteolysis and disulfide bond formation. That latter protein modification, which very often influences the tertiary and quaternary structure of virulence determinants, plays an important role in bacterial pathogenesis [15, 16]. In Gram-negative bacteria disulfide bond check details formation is facilitated by the Dsb (disulfide bond) family of

redox proteins, which function in the periplasmic space under oxidizing conditions. In E. coli the disulfide bridge formation system operates in two partially coinciding metabolic pathways: the oxidation (DsbA and DsbB) pathway and the isomerization/reduction (DsbC and DsbD) pathway. The oxidation pathway is responsible for the formation of disulfide bonds in newly synthesized proteins, just after they cross the cytoplasmic membrane. This process occurs in a rather non-selective way. The isomerization/reduction pathway rearranges improperly 4-Aminobutyrate aminotransferase introduced disulfides [15, 16]. The sequencing of more and more bacterial genomes has revealed that the process of disulfide bond formation in bacteria is extremely diverse, and it has become obvious that E. coli Dsb system cannot be considered a paradigm for Dsb activity [16, 17]. The Dsb oxidative pathway of C. jejuni is much more complex than the oxidative pathway of the laboratory E. coli K-12. Depending on the strain, it is catalyzed by three or four enzymes – two localized in the inner membrane (DsbB and DsbI) and one or two in the periplasm (DsbA1 and DsbA2).