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D’Costa, Vanessa M.; Braun, Virginie; Landekic, Marija; Shi, Rong; Proteau, Ariane; McDonald, Laura; Cygler, Miroslaw; Grinstein, Sergio; Brumell, John H.
Cell reports (Cambridge), 09/2015, Volume: 12, Issue: 9Journal Article
Intracellular bacterial pathogens of a diverse nature share the ability to evade host immunity by impairing trafficking of endocytic cargo to lysosomes for degradation, a process that is poorly understood. Here, we show that the Salmonella enterica type 3 secreted effector SopD2 mediates this process by binding the host regulatory GTPase Rab7 and inhibiting its nucleotide exchange. Consequently, this limits Rab7 interaction with its dynein- and kinesin-binding effectors RILP and FYCO1 and thereby disrupts host-driven regulation of microtubule motors. Our study identifies a bacterial effector capable of directly binding and thereby modulating Rab7 activity and a mechanism of endocytic trafficking disruption that may provide insight into the pathogenesis of other bacteria. Additionally, we provide a powerful tool for the study of Rab7 function, and a potential therapeutic target. Display omitted •The effector SopD2 blocks delivery of endocytic cargo to lysosomes•SopD2 interacts directly with host GTPase Rab7•SopD2’s N terminus mediates both trafficking suppression and interaction with Rab7•SopD2 impairs Rab7’s ability to bind cognate effectors RILP and FYCO1 Intracellular pathogens can evade host immunity by impairing trafficking of endocytic cargo to lysosomes for degradation. D’Costa et al. show that the effector SopD2 mediates this process in Salmonella infection by binding the host regulatory GTPase Rab7 and impairing its ability to recruit dynein- and kinesin-binding effectors RILP and FYCO1.
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