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Chlamydophila (Cp.) psittaci , the causative agent of psittacosis in birds and humans, is the most important zoonotic pathogen of the family  Chlamydiaceae . These obligate intracellular bacteria are distinguished by a unique biphasic developmental cycle, which includes proliferation in a membrane-bound compartment termed inclusion. All  Chlamydiaceae spp.  possess a coding capacity for core components of a Type III secretion apparatus, which mediates specific delivery of anti-host effector proteins either into the chlamydial inclusion membrane or into the cytoplasm of target eukaryotic cells. Here we describe the interaction between Type III-secreted protein IncA of  Cp. psittaci  and host protein G3BP1 in a yeast two-hybrid system. In GST-pull down and co-immunoprecipitation experiments both  in vitro  and  in vivo  interaction between full-length IncA and G3BP1 were shown. Using fluorescence microscopy, the localization of G3BP1 near the inclusion membrane of  Cp. psittaci -infected Hep-2 cells was demonstrated. Notably, infection of Hep-2 cells with  Cp. psittaci  and overexpression of IncA in HEK293 cells led to a decrease in c-Myc protein concentration. This effect could be ascribed to the interaction between IncA and G3BP1 since overexpression of an IncA mutant construct disabled to interact with G3BP1 failed to reduce c-Myc concentration. We hypothesize that lowering the host cell c-Myc protein concentration may be part of a strategy employed by  Cp. psittaci  to avoid apoptosis and scale down host cell proliferation.

Functional Interaction between Type III-Secreted Protein IncA of Chlamydophila psittaci and Human G3BP1