Obligate intracellular bacterial pathogens, like Coxiella burnetii, the causative agent of Q Fever, rely upon the host for metabolites and carbon sources for energy and biosynthesis of nucleic acids, proteins, and energy rich molecules necessary for active vegetative growth in the host. Deficiencies in biosynthetic pathways were previously identified through genomic analyses of C. burnetii, but bacterial factors contributing to pathogenesis, with the exception of the O-lipopolysaccharide (O-LPS) and the Type IVb Secretion System (T4BSS), remain elusive. The poor efficacy of treatment and vaccine options necessitates understanding how bacterial factors contribute to disease severity, persistence of infections, and inconsistent treatment outcomes. Disulfide bond (Dsb) proteins are integral in the formation and isomerization of disulfide bonds in the T4bSS. Dsb proteins in other bacterial pathogens act upon known virulence factors that promote pathogenicity. The purpose of this study was to characterize the Coxiella outer membrane protein 1 (Com1), a putative Dsb protein, establish that it is a functional Dsb protein, and that it is linked to known virulence factors. This work will deepen the understanding in the Coxiella field of factors that might serve as alternative targets for therapeutics.Includes bibliographical references
