The role of chlamydial proteases in the pathogenesis of Chlamydia spp. has remained largely unknown. In the present study we have generated a Chlamydia muridarum strain that is a null mutant of tail specific protease (TSP). TSP has conserved orthologs in other chlamydial species and structurally similar homologs in multiple free-living and intracellular bacteria. Similar to the roles of its homologs, TSP seems to play a crucial role in chlamydial resistance to elevated temperatures. Importantly, the tsp null mutant is also heavily attenuated in the mouse urogenital tract, indicating that TSP has a crucial role in chlamydial pathogenicity. We have utilized quantitative proteomics to identify chlamydial proteins that have altered abundances in the tsp null mutant compared to wild-type and an isogenic recombinant of the mutant. These proteins indicate potential substrates of this protease and hints toward the molecular function of TSP.
[doi:10.25345/C5H41JR7S]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: chlamydia ; tail specific protease ; LC-MS/MS
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Amber L. Mosley, Indiana University School of Medicine, USA David E. Nelson, Indiana University School of Medicine, USA |
Submitting User: | edoud |
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