Probing the role of protein surface charge in the activation of PrfA, the central regulator of Listeria monocytogenes pathogenesis.

ABSTRACT: Listeria monocytogenes is a food-borne intracellular bacterial pathogen capable of causing serious human disease. L. monocytogenes survival within mammalian cells depends upon the synthesis of a number of secreted virulence factors whose expression is regulated by the transcriptional activator PrfA. PrfA becomes activated following bacterial entry into host cells where it induces the expression of gene products required for bacterial spread to adjacent cells. Activation of PrfA appears to occur via the binding of a small molecule cofactor whose identity remains unknown. Electrostatic modeling of the predicted PrfA cofactor binding pocket revealed a highly positively charged region with two lysine residues, K64 and K122, located at the edge of the pocket and another (K130) located deep with

SUBMITTER: Xayarath B 

PROVIDER: S-EPMC3155570 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature