INVESTIGADORES
CAPMANY anahi
congresos y reuniones científicas
Título:
Chlamydia trachomatis RECRUITS Rab39, A NOVEL GOLGI-ASSOCIATED GTPase
Autor/es:
GAMBARTE J; CAPMANY A; LEIVA N; DAMIANI MT
Lugar:
Potrero de los Funes, San Luis
Reunión:
Congreso; XLVII Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2011
Institución organizadora:
SAIB
Resumen:
Chlamydia trachomatis is an obligate intracellular Gram-negativebacterium, which multiplies in a single vacuole called inclusion.This bacterium early dissociates from the endocytic pathway butcontinues the interaction with the biosynthetic route. Thisbacterium intercepts vesicles full of nutrients departed from theGolgi apparatus essential for its survival and development. We havedescribed that Chlamydia re-directs Rab11- and Rab14-mediatedvesicular transport to capture endogenous lipids synthesized in theGolgi. Rab39 is a recently described host GTPase, localized at theGolgi apparatus, which precise function is still poorly understood.The aim of this study was to investigate if Chlamydia manipulatesRab39-mediated vesicular trafficking for its own nutrition andbenefit. Cells overexpressing Rab39a wt and its negative mutant:Rab39a S25N (a GDP-bound inactive form) and its positivemutant: Rab39a Q70L (a GTP-anchored active form) wereanalyzed by confocal and electron microscopy after bacterialinfection. Our results showed that Rab39a wt is recruited to thechlamydial membrane inclusion in a time-dependent fashion.Furthermore, our results demonstrated that Rab39b wt, an isoformof Rab39a wt, did not display the same pattern of recruitment.These results suggest that host Rab39a-mediated transport issubverted by Chlamydia trachomatis to generate a safe intracellularniche where survive and replicate.