Rin1 restores host phagocytosis activity during the invasion of Pseudomonas aeruginosa

Journal of Medical Microbiology
Sushmita Mustafi, M A Barbieri

Abstract

Pseudomonas aeruginosa uses Type III secretion system to deliver toxic effector proteins directly into host cells and alter host protein functions. Exoenzyme S (ExoS), a Type III effector protein, ADP-ribosylates Rab5 GTPase and impair early phagocytic events in macrophage cells. In this current study, we tested the hypothesis that Rin1, a Ras effector protein and Rab5 guanine exchange factor (GEF), generates an intrinsic Rab5 activity cycle during phagocytosis of live P. aeruginosa thus allowing proper phagocytic killing. We found that Rab5 activity was attenuated at a very early time point (2.5 min) of the phagocytic process of live but not of heat inactivated P. aeruginosa. However, upon overexpressing Rin1 in macrophages, the Rab5 activity sustained for a prolonged time (~20 min) counteracting the negative effect during phagocytosis of live P. aeruginosa. Ras, also a substrate of ADP-ribosyltransferase activity of ExoS, remained active during the early events of phagocytosis of live as well as heat inactivated P. aeruginosa. Further examinations revealed that Rin1:Vps9 domain (the Rab5 nucleotide catalytic domain) and Rin1:RA domain (the Ras association domain of Rin1) are both required for optimal Rin1 function. Finally, t...Continue Reading

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