The GTPase Rab14 is recruited to Chlamydia trachomatis inclusion.

CAPMANY A,; PAVAROTTI M,; LEIVA N,; POCOGNONI C,; DAMIANI MT.

Carlos Paz, Córdoba, Argentina

Congreso; XLIV Reunión Científica Anual de la Soc. Argentina de Investigación en Bioquímica y Biología Molecular SAIB; 2008

Soc. Argentina de Investigación en Bioquímica y Biología Molecular - SAIB

Chlamydia trachomatis is a Gram-negative obligate intracellular bacterium that causes genital and ocular infections in humans. This bacterium replicates in an inclusion that is trafficked to the peri-Golgi region. This inclusion receives material from the biosynthetic via by fusing with vesicles released from the TGN. The specific host and bacterial factors that mediate this intracellular trafficking to the chlamydia vacuole remain undefined. Rab GTPases are the molecules in charge of controlling intracellular transport. Since Rab14 is a key regulator of vesicular transport between the TGN and early endosomes, and is critical for the maintenance of Mycobacterium tuberculosis phagosome maturation arrest; we postulate that Rab14 is involved in chlamydia inclusion development. We examine by confocal microscopy the intracellular localization and function of this Rab and its inactive mutants: Rab14 S25N (Rab14 GDP-bound form) and Rab14 DGCGC (Rab14 not associated to membranes) fused to EGFP in Hela cells infected with C. trachomatis biovar LGV. We observed a marked recruitment of EGFP- Rab14 to the membrane of chlamydia inclusions. These data suggest that Chlamydia trachomatis selectively interferes with critical components of the trafficking machinery of the host cell in order to generate an intracellular niche favorable for its surviving and development.