Comparative proteomics of Chlamydia muridarum strains in the absence of the conserved tail specific protease
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ABSTRACT: 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.
INSTRUMENT(S): Orbitrap Fusion Lumos
ORGANISM(S): Mus Musculus (ncbitaxon:10090) Chlamydia Muridarum (ncbitaxon:83560)
SUBMITTER: David E. Nelson Amber L. Mosley
PROVIDER: MSV000090509 | MassIVE | Mon Oct 10 12:50:00 BST 2022
SECONDARY ACCESSION(S): PXD037282
REPOSITORIES: MassIVE
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