Structural Analysis of PhoQ

 

Salmonellae utilize the PhoPQ two-component system to sense and survive within the host intracellular environment. The PhoQ histidine kinase has a periplasmic sensor domain which is regulated by divalent cations and activated by acidic pH and cationic antimicrobial peptides (CAMP). Using a combination of structural, biochemical, and in vivo methods we are characterizing distinct subdomain networks within the PhoQ periplasmic domain which are involved in signal transduction. Ultimately, our efforts will provide a structural model of the PhoQ activation mechanism.

Publications:

1. Rader, B.A., Wreden, C., Hicks, K.G., Sweeney, E.G., Ottemann, K.M., and Guillemin, K. (2011). Helicobacter pylori perceives the quorum-sensing molecule AI-2 as a chemorepellant via the chemoreceptor TlpB. Microbiology.

2. Hood, R.D., Singh, P., Hsu, F., Guvener, T., Carl, M.A., Trinidad, R.R., Silverman, J.M., Ohlson, B.B., Hicks, K.G., Plemel, R.L., et al. (2010). A type VI secretion system of Pseudomonas aeruginosa targets a toxin to bacteria. Cell host & microbe 7, 25-37.