The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis.

ABSTRACT: Listeria monocytogenes is an intracellular bacterial pathogen whose virulence depends on the regulated expression of numerous secreted bacterial factors. As for other gram-positive bacteria, many proteins secreted by L. monocytogenes are translocated across the bacterial membrane in an unfolded state to the compartment existing between the membrane and the cell wall. This compartment presents a challenging environment for protein folding due to its high density of negative charge, high concentrations of cations, and low pH. We recently identified PrsA2 as a gene product required for L. monocytogenes virulence. PrsA2 was identified based on its increased secretion by strains containing a mutationally activated form of prfA, the key regulator of L. monocytogenes virulence gene expression. Th

SUBMITTER: Alonzo F 

PROVIDER: S-EPMC2708592 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature