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A more recent version of this article appeared on September 1, 2005
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Submitted on April 29, 2005
Revised on June 16, 2005
Accepted on June 17, 2005
Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840
Monitoring Editor: Ralph Isberg
After internalization into mammalian cells, the bacterial pathogen, Salmonella enterica, resides within a membrane-bound compartment, the Salmonella-containing vacuole (SCV). During its maturation process, the SCV interacts extensively with host cell endocytic compartments, especially late endosomes/lysosomes (LE/Lys) at later stages. These interactions are mediated by the activities of multiple bacterial and host cell proteins. Here we show that the Salmonella type III effector, PipB2, reorganizes LE/Lys compartments in mammalian cells. This activity results in the centrifugal extension of lysosomal glycoprotein (lgp)-rich membrane tubules, known as Sifs, away from the SCV along microtubules. Salmonella overexpressing pipB2 induce the peripheral accumulation of LE/Lys compartments, reducing the frequency of LE/Lys tubulation. Furthermore, ectopic expression of pipB2 redistributes LE/Lys, but not other cellular organelles, to the cell periphery. In coexpression studies, PipB2 can overcome the effects of dominant-active Rab7 or Rab34 on LE/Lys positioning. Deletion of a C-terminal pentapeptide motif of PipB2, LFNEF, prevents its peripheral targeting and effect on organelle positioning. The PipB2 homologue, PipB, does not possess this motif or the same biological activity as PipB2. Therefore, it appears that a divergence in the biological functions of these two effectors can be accounted for by sequence divergence in their C-termini.
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