Further, via fluorescent immunohistochemistry, we noted abundant localization of these proteins within key functional areas of primary human placental tissues, namely the outer syncytial layer of placental villous tissue and the endothelia of fetal blood vessels. We also identified the expression of these proteins in human placental lysates by Western blot analysis. By immunofluorescence microscopy, Rab11a, Rab11c( Rab25), Rab14 as well as their common FIP effector RCP showed prominent expression in the placental cell lines. As Rab11 proteins are closely involved in transcytosis we hypothesized that the placenta would be an interesting human tissue model system for Rab investigation. The placenta is a highly active exchange interface, facilitating transfer between mother and fetus during pregnancy. These findings encouraged us to further analyse the localization of these Rabs and their common effector protein, the Rab Coupling Protein (RCP), by immunofluorescence microscopy and to extend this work to normal human placental tissue. The results from this analysis indicated that Rab11a, Rab11c( Rab25) and Rab14 were expressed in a wide range of cell lines, including the human placental trophoblastic BeWo cell line.
In an effort to further study these proteins, we conducted a preliminary investigation of a subgroup of endosomal Rab proteins in a range of human cell lines by Western blotting. While the Rab11 subfamily has been well characterized at the cellular level, its function within human organ systems is still being explored.
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This Rab subfamily works through a series of effector proteins including the Rab11-FIPs ( Rab11 Family-Interacting Proteins). The Rab11 subfamily in particular directs key steps of intracellular functions involving vesicle trafficking of the endosomal recycling pathway. Rab proteins are a family of small GTPases involved in a variety of cellular processes.
Wuebbolt, Danielle Breathnach, Fionnuala M. Rab11 family expression in the human placenta: Localization at the maternal-fetal interfaceĪrtemiuk, Patrycja A.
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C. trachomatis likely recruits FIP2 to hijack host intracellular trafficking to redirect vesicles full of nutrients towards the inclusion. In agreement, the silencing of FIP2 decreases the bacterial progeny. Furthermore, our results show that FIP2 promotes inclusion development and bacterial replication. The presence of FIP2 at the chlamydial inclusion favours the recruitment of Rab14. Our results indicate that FIP2 binds to Rab11 at the chlamydial inclusion membrane through its Rab-binding domain. The Rab-binding domain of FIP2 is essential for its association. The recruitment of FIP2 is specific since other members of the Rab11- Family of Interacting Proteins do not associate with the chlamydial inclusions. In this study, we determined and characterized the recruitment of endogenous and GFP-tagged FIP2 to the chlamydial inclusions. FIP2, a member of the Rab11- Family of Interacting Proteins, presents at the C-terminus a Rab-binding domain that interacts with both Rab11 and Rab14. Several Rabs, among them Rab11 and Rab14, are implicated in chlamydial development. Rab GTPases are key regulatory proteins of intracellular trafficking. Leiva, Natalia Capmany, Anahà Damiani, MarÃa TeresaĬhlamydia trachomatis, an obligate intracellular pathogen, survives within host cells in a special compartment named 'inclusion' and takes advantage of host vesicular transport pathways for its growth and replication. Rab11- family of interacting protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication.
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