Serine/threonine protein kinase PpkA contributes to the adaptation and virulence in Pseudomonas aeruginosa.

Pseudomonas aeruginosa is a leading cause of nosocomial infections worldwide and has become a serious public health threat, which is attributed to a large extent to its extraordinary environmental adaptability and diverse virulence factors that result in infection and progression of pathogenesis. The eukaryote-type serine/threonine (Ser/Thr) protein kinases, known for playing major regulatory roles in eukaryotes, have been demonstrated to play a central role in regulating various bacterial cellular processes via catalyzing protein phosphorylation. Although PpkA, a Ser/Thr protein kinase first identified in P. aeruginosa, has been implicated in association with bacterial virulence, little is known about the protein. Therefore, in this study, to assess the potential role of PpkA in the regulation of P. aeruginosa environmental adaptation and virulence, variations of biofilm formation, pyocyanin production, tolerance to stress, cell invasion and plant virulence were determined in wild type PAO1, ppkA gene-deleted and complemented mutant strains. Our results indicate that the mutant strain lacking ppkA exhibited a significant decrease of biofilm formation and pyocyanin production, less tolerance to oxidative and osmotic stresses, inefficient invasion of host cells and a reduction of bacterial virulence. These findings provide new insight into the regulation of various cellular processes by PpkA; this is an important mechanism for adaptation and virulence in P. aeruginosa.