INVESTIGADORES
LEIVA natalia lorena
congresos y reuniones científicas
Título:
Chlamydia trachomatis intercepts Rab39-mediated vesicular trafficking
Autor/es:
GAMBARTE J; CAPMANY A; QUINTERO C; LEIVA N; GOUD B; DAMIANI MT
Lugar:
Ciudad de Mendoza. Mendoza
Reunión:
Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB).; 2012
Institución organizadora:
SAIB
Resumen:
The intracellular pathogen Chlamydia trachomatis, replicates
within a special compartment limited by membranes (called
"inclusion") and takes advantage of host vesicular transport for its
own benefit. Rab GTPases are key regulatory proteins of
intracellular trafficking. We have demonstrated that Rab11, Rab14
and Rab11-Interacting Protein 2 (FIP2) are recruited to chlamydial
inclusions and, are necessary for bacterial multiplication. Recently,
it has been described that FIP2 encompasses, at its C-terminus, a
Rab Binding Domain (RBD) that interacts with both, Rab11 and
Rab14. The aim of this study was to assess the interplay between
these three host proteins in infected cells. The degree of
colocalization at the chlamydial inclusion membrane was measured
by quantitative confocal microscopy. Manders´ and Pearson´s
coefficients indicated almost complete colocalization between these
proteins, even after Golgi disorganization or depolymerization of
microtubules. Overexpression of the Rab11 GDP-bound mutant
(Rab11-S25N) decreased the recruitment of FIP2, whereas the
overexpression of the FIP2 mutant lacking the RBD
(FIP2 C2 RBD) did not affect Rab11 association with chlamydial
inclusions. On the contrary, the silencing of FIP2 diminished the
binding of Rab14. These results might suggest that FIP2 coordinates
the sequential recruitment of Rab11 and Rab14 to chlamydial inclusions.
within a special compartment limited by membranes (called
"inclusion") and takes advantage of host vesicular transport for its
own benefit. Rab GTPases are key regulatory proteins of
intracellular trafficking. We have demonstrated that Rab11, Rab14
and Rab11-Interacting Protein 2 (FIP2) are recruited to chlamydial
inclusions and, are necessary for bacterial multiplication. Recently,
it has been described that FIP2 encompasses, at its C-terminus, a
Rab Binding Domain (RBD) that interacts with both, Rab11 and
Rab14. The aim of this study was to assess the interplay between
these three host proteins in infected cells. The degree of
colocalization at the chlamydial inclusion membrane was measured
by quantitative confocal microscopy. Manders´ and Pearson´s
coefficients indicated almost complete colocalization between these
proteins, even after Golgi disorganization or depolymerization of
microtubules. Overexpression of the Rab11 GDP-bound mutant
(Rab11-S25N) decreased the recruitment of FIP2, whereas the
overexpression of the FIP2 mutant lacking the RBD
(FIP2 C2 RBD) did not affect Rab11 association with chlamydial
inclusions. On the contrary, the silencing of FIP2 diminished the
binding of Rab14. These results might suggest that FIP2 coordinates
the sequential recruitment of Rab11 and Rab14 to chlamydial inclusions.
Chlamydia trachomatis, replicates
within a special compartment limited by membranes (called
"inclusion") and takes advantage of host vesicular transport for its
own benefit. Rab GTPases are key regulatory proteins of
intracellular trafficking. We have demonstrated that Rab11, Rab14
and Rab11-Interacting Protein 2 (FIP2) are recruited to chlamydial
inclusions and, are necessary for bacterial multiplication. Recently,
it has been described that FIP2 encompasses, at its C-terminus, a
Rab Binding Domain (RBD) that interacts with both, Rab11 and
Rab14. The aim of this study was to assess the interplay between
these three host proteins in infected cells. The degree of
colocalization at the chlamydial inclusion membrane was measured
by quantitative confocal microscopy. Manders´ and Pearson´s
coefficients indicated almost complete colocalization between these
proteins, even after Golgi disorganization or depolymerization of
microtubules. Overexpression of the Rab11 GDP-bound mutant
(Rab11-S25N) decreased the recruitment of FIP2, whereas the
overexpression of the FIP2 mutant lacking the RBD
(FIP2 C2 RBD) did not affect Rab11 association with chlamydial
inclusions. On the contrary, the silencing of FIP2 diminished the
binding of Rab14. These results might suggest that FIP2 coordinates
the sequential recruitment of Rab11 and Rab14 to chlamydial inclusions.