Pseudomonas aeruginosa is a biofilm-forming, gram-negative bacteria that is the main causative agent of lung infections in patients with cystic fibrosis. Biofilms are multicellular communities formed when bacteria attach to a surface and secrete a thick, mucoid protective barrier known as the exopolymeric substance, which is mostly composed of polysaccharides extracellular DNA, and proteins. Due to these biofilm properties, P. aeruginosa has been classified as a number one priority in need of a new antibiotic/treatment by the World Health Organization. It has previously been shown that the diatomic gas, nitric oxide (NO), mediates biofilm dispersal. Our lab investigates the NO sensing protein (NosP) and its co-cistronic associated histidine kinase (NahK). NosP has previously been shown to induce biofilm dispersal by inhibiting the kinase activity of NahK. In P. aeruginosa, NahK has been shown to phosphorylate a histidine phosphotransfer protein (HptB), which acts a phosphorelay hub for multiple, complex two component signal transduction systems. However, preliminary data has revealed several observed phenotypes independent of direct HptB signaling; thus, suggesting the involvement of NahK in other signaling cascades. In P. aeruginosa, NahK is a cytosolic, sensory hybrid histidine kinase containing three uncharacterized N-terminal PAS signaling domains. We hypothesize that the signaling domains provide a secondary regulatory system over kinase activity, separate from the NO-mediated regulation through NosP, resulting in biofilm dispersal through the downstream effects of the HptB phosphorelay system and secondary signaling cascades.

Functional characterization of the NosP associated histidine kinase, NahK, and its role in biofilm regulation in <i>Pseudomonas aeruginosa</i>

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Functional characterization of the NosP associated histidine kinase, NahK, and its role in biofilm regulation in Pseudomonas aeruginosa