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MATERIALS & METHODS

 MICROSCOPIC TECHNIQUES SPECIES MORPHOLOGY CELL LINE
616 The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor Takahiro Murata, Anna Delprato, Alyssa Ingmundson, Derek K. Toomre, David G. Lambright
and Craig R. Roy		 Legionella pneumophila, membrane transport, endoplasmic reticulum, bacterial replication, Golgi apparatus, GTPases, vesicular transport

For multi-channel TIRFM, CHO Fc?RII cells grown in 35-mm glass bottom dishes (MatTek, Ashland, MA)…

 immunofluorescence microscopy chinese hamster CHO Fc?RII
Abstract
  The intracellular pathogen Legionella pneumophila avoids fusion with lysosomes and subverts membrane transport from the endoplasmic reticulum to create an organelle that supports bacterial replication1,2. Transport of endoplasmic reticulumderived vesicles to the Legionella-containing vacuole (LCV) requires bacterial proteins that are translocated into host cells by a type IV secretion apparatus called Dot/Icm3–7. Recent observations have revealed recruitment of the host GTPase Rab1 to the LCV by a process requiring the Dot/Icm system8,9. Here, a visual screen was used to identify L. pneumophila mutants with defects in Rab1 recruitment. One of the factors identified in this screen was DrrA, a new Dot/Icm substrate protein translocated into host cells. We show that DrrA is a potent and highly specific Rab1 guanine nucleotide-exchange factor (GEF). DrrA can disrupt Rab1-mediated secretory transport to the Golgi apparatus by competing with endogenous exchange factors to recruit and activate Rab1 on plasma membrane-derived organelles. These data establish that intracellular pathogens have the capacity to directly modulate the activation state of a specific member of the Rab family of GTPases and thus further our understanding of the mechanisms used by bacterial pathogens to manipulate host vesicular transport.  

 

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