Chlamydia trachomatis INTERCEPTS Rab39-MEDIATED VESICULAR TRAFFICKING

GAMBARTE J; CAPMANY A; QUINTERO C; LEIVA N; GOUD B

Mendoza

Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2012

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB)

Chlamydia trachomatis is a bacterial causative agent of major sexually-transmitted diseases and blindness in humans. During its development, this obligate intracellular bacterium resides and multiplies in a modified vacuole called inclusion C. trachomatis subverts key eukaryotic proteins in charge of vesicular transport to prevent its degradation by phagocytosis, and simultaneously, to obtain nutrients from parasitized cells. Rab GTPases are master controllers of intracellular trafficking pathways, which cycle between a GTP-bound form (active) to a GDP-bound form (inactive). The aim of this study was to investigate if manipulates host Rab39-mediated vesicular trafficking. We observed that Rab39a associated with the chlamydial inclusion along its developing time. Rab39a colocalized with IncA and IncG, two bacterial proteins, at the chlamydial inclusion membrane. We determined that the recruitment of Rab39a is bacterial protein synthesis-dependent. Furthermore, Rab39a recruitment to the inclusions remains unaltered after treatment with drugs that interferes with the cytoskeleton, such as nocodazole, butanedionemonoxime and cytochalasin. Rab39a decorated vesicles carrying sphingolipids and labeled with lysotracker in infected cells. Furthermore, overexpression of Rab39a WT and its positive mutant Rab39a Q72L increased the chlamydial inclusion size. Therefore, these results suggest a potential role for Rab39 in chlamydial infection outcome.