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Rickettsia typhi , the causative agent of murine (endemic) typhus, is an obligate intracellular pathogen with a life cycle involving both vertebrate and invertebrate hosts. In this study, we characterized a gene (RT0218 ) encoding a C-terminal ankyrin repeat domain-containing protein, namedR ickettsia a nkyrinr epeatp rotein 1 (RARP-1), and identified it as a secreted effector protein ofR. typhi .RT0218 showed differential transcript abundance at various phases ofR. typhi intracellular growth. RARP-1 was secreted byR. typhi into the host cytoplasm duringin vitro infection of mammalian cells. Transcriptional analysis revealed thatRT0218 was cotranscribed with adjacent genesRT0217 (hypothetical protein) andRT0216 (TolC) as a single polycistronic mRNA. Given one of its functions as a facilitator of extracellular protein secretion in some Gram-negative bacterial pathogens, we tested the possible role of TolC in the secretion of RARP-1. UsingEscherichia coli C600 and an isogenictolC insertion mutant as surrogate hosts, our data demonstrate that RARP-1 is secreted in a TolC-dependent manner. Deletion of either the N-terminal signal peptide or the C-terminal ankyrin repeats abolished RARP-1 secretion by wild-typeE. coli . Importantly, expression ofR. typhi tolC in theE. coli tolC mutant restored the secretion of RARP-1, suggesting that TolC has a role in RARP-1 translocation across the outer membrane. This work implies that the TolC component of the putative type 1 secretion system ofR. typhi is involved in the secretion process of RARP-1.

TolC-Dependent Secretion of an Ankyrin Repeat-Containing Protein of Rickettsia typhi