Abstract
Intracellular bacterial pathogens survive and replicate within specialized eukaryotic cell organelles. To establish their intracellular niches these pathogens have adopted sophisticated strategies to control intracellular membrane trafficking. Since Rab-family GTPases are critical regulators of endocytic and secretory membrane trafficking events, many intracellular pathogens have evolved specific mechanisms to modulate or hijack Rab GTPases dynamics and trafficking functions. One such strategy is the delivery of bacterial effectors through specialized machines to specifically target Rab GTPases. Some of these effectors functionally mimic host proteins that regulate the Rab GTP cycle, while others regulate Rabs proteins through their post-translation modifications or proteolysis. In this review, we examine how the localization and function of Rab-family GTPases are altered during infection with 3 well-studied intracellular bacterial pathogens, Mycobacterium tuberculosis, Salmonella enterica and Legionella pneumophila. We also discuss recent findings about specific mechanisms by which these intracellular pathogens target this protein family.