The Rab11 interacting protein FIP-2 is recruited to Chlamydia trachomatis inclusion

LEIVA N; CAPMANY A; PAVAROTTI M; DAMIANI MT

San Miguel de Tucuman,Tucuman, Argentina.

Congreso; XLV Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular. SAIB; 2009

Sociedad Argentina de Investigacion en. Bioquímica y Biología Molecular (SAIB)

Chlamydia trachomatis is an obligate intracellular bacterium that replicates in a not acidic vacuole called inclusion. Rab GTPases are the molecules in charge of intracellular traffic control. Rab11, a Rab present on immature phagosomes, is recruited towards the inclusion of Chlamydia. A Rab11-Family of interacting Proteins known as FIPs has recently been cloned. Rab11-FIP2 has a RBD (Rab11/25 Binding Domain) domain in its C-terminus which interacts with Rab11 and a C2 domain in its N-terminus that binds phospholipids. We are interested on unravel Rab11-FIP2 involvement in Chlamydia trachomatis inclusion biogenesis and development. We examined by confocal microscopy the intracellular localization and function of this interacting protein and its mutants: Rab11-FIP2∆C2 and Rab11-FIP2∆C2∆RBD fused to EGFP in Hela cells infected with C. trachomatis biovar LGV. We observed that this protein strongly decorates Chlamydia inclusion, whereas Rab11-FIP2ÄC2∆RBD, the mutant that lacks the RBD domain, is not found associated to it. FIP2WT recruitment occurs at early stages of inclusion development, and depends on bacterial protein synthesis. 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.