INVESTIGADORES
LEIVA Natalia Lorena
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 (SAIB); 2011
Institución organizadora:
SAIB
Resumen:
Chlamydia trachomatis is an obligate intracellular Gram-negative
bacterium, which multiplies in a single vacuole called inclusion.
This bacterium early dissociates from the endocytic pathway but
continues the interaction with the biosynthetic route. This
bacterium intercepts vesicles full of nutrients departed from the
Golgi apparatus essential for its survival and development. We have
described that Chlamydia re-directs Rab11- and Rab14-mediated
vesicular transport to capture endogenous lipids synthesized in the
Golgi. Rab39 is a recently described host GTPase, localized at the
Golgi apparatus, which precise function is still poorly understood.
The aim of this study was to investigate if Chlamydia manipulates
Rab39-mediated vesicular trafficking for its own nutrition and
benefit. Cells overexpressing Rab39a wt and its negative mutant:
Rab39a S25N (a GDP-bound inactive form) and its positive
mutant: Rab39a Q70L (a GTP-anchored active form) were
analyzed by confocal and electron microscopy after bacterial
infection. Our results showed that Rab39a wt is recruited to the
chlamydial membrane inclusion in a time-dependent fashion.
Furthermore, our results demonstrated that Rab39b wt, an isoform
of Rab39a wt, did not display the same pattern of recruitment.
These results suggest that host Rab39a-mediated transport is
subverted by Chlamydia trachomatis to generate a safe intracellular
niche where survive and replicate.
bacterium, which multiplies in a single vacuole called inclusion.
This bacterium early dissociates from the endocytic pathway but
continues the interaction with the biosynthetic route. This
bacterium intercepts vesicles full of nutrients departed from the
Golgi apparatus essential for its survival and development. We have
described that Chlamydia re-directs Rab11- and Rab14-mediated
vesicular transport to capture endogenous lipids synthesized in the
Golgi. Rab39 is a recently described host GTPase, localized at the
Golgi apparatus, which precise function is still poorly understood.
The aim of this study was to investigate if Chlamydia manipulates
Rab39-mediated vesicular trafficking for its own nutrition and
benefit. Cells overexpressing Rab39a wt and its negative mutant:
Rab39a S25N (a GDP-bound inactive form) and its positive
mutant: Rab39a Q70L (a GTP-anchored active form) were
analyzed by confocal and electron microscopy after bacterial
infection. Our results showed that Rab39a wt is recruited to the
chlamydial membrane inclusion in a time-dependent fashion.
Furthermore, our results demonstrated that Rab39b wt, an isoform
of Rab39a wt, did not display the same pattern of recruitment.
These results suggest that host Rab39a-mediated transport is
subverted by Chlamydia trachomatis to generate a safe intracellular
niche where survive and replicate.