Tetramer formation of CpoS facilitates Inc-Inc interactions during Chlamydia trachomatis infection
Year: 2024
Type: preprint
Abstract: Chlamydia trachomatis ( C.t. ), the leading bacterial cause of sexually transmitted infections, replicates within a unique intracellular compartment called the inclusion, which is modified by secreted proteins known as inclusion membrane (Inc) proteins. Here we further characterize CpoS, an Inc previously shown to be critical for replication and inclusion development. We demonstrate that CpoS directly binds multiple coiled-coil domain-containing Incs while simultaneously engaging Rab GTPases at a separate site. Notably, CpoS-InaC interactions facilitate the recruitment of select Arfs to the inclusion membrane, while Rab recruitment occurs independtly of these interactions. Biochemical and biophysical analyses revealed that Incs self-oligomerize, forming higher-ordered structures, with CpoS adpoting a tetrameric structure resembling eukaryotic SNAREs. We propose these assemblies likely serve as scaffolds to orchestrate vesicle docking, tethering, and fusion. Our findings underscore the intricate interplay between bacterial and host factors, revealing that C.t. leverages both Inc-Inc interactions and host protein engagement to manipulate vesicular trafficking and sustain infection.
Institution: University of Iowa
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W4404897187