Chlamydia interacts with the Golgi apparatus - understanding the underlying molecular mechanisms

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Chlamydia spp. are obligate intracellular bacterial pathogens. Inside the eukaryotic host cell they are found in a membrane-bound compartment called the inclusion. Little is known about the molecular basis for specific interactions between this bacterial niche and cellular compartments, including the Golgi apparatus (GA). We have recently demonstrated that infection with C. trachomatis causes fragmentation of the GA, which is accompanied by processing of an important cellular Golgi matrix protein, golgin-84. Knockdown of the two GTPases, Rab6A and Rab11A, by RNA interference (RNAi) inhibited Chlamydia-induced and golgin-84-dependent Golgi fragmentation indicating that Rab proteins and golgin-84 are linked in a pathway that contributes to Golgi structure. Furthermore, our published data support the hypothesis that Golgi fragmentation is essential for bacterial lipid acquisition and Chlamydia growth. We will study trafficking of photoactivatable Rab6A, Rab11A and golgin-84 fusion proteins by confocal live cell microscopy to understand the dynamics of these proteins in infected and control cells. Characterization of Rab and golgin-84 interaction partners (known and novel) by biochemical means and RNAi will be used to elucidate the role of these factors in Chlamydia-induced Golgi fragmentation, bacterial lipid acquisition and development. The aim of the study is to understand the molecular basis of the processes by which Rab proteins and golgins cause Golgi fragmentation in infected cells to ensure Chlamydia lipid acquisition and growth.