Philadelphia University + Thomas Jefferson University

Publications

Highlighted Publications

J. Wesolowski, MM. Weber, A. Nawrotek, CA. Dooley, M. Calderon, CM. St. Croix, T. Hackstadt, J. Cherfils, F. Paumet (2017) Chlamydia Hijacks ARF GTPases To Coordinate Microtubule Posttranslational Modifications and Golgi Complex Positioning” mBio 8: e02280-16

This study provides the first evidence that a chlamydial protein CT813 recruits the GTPases ARF1 and ARF4, which in turn play a critical role in controlling post-translationally modified microtubules around the inclusion. Furthermore, this study demonstrates that Chlamydia trachomatis hijacks this novel function of ARF to reposition the Golgi mini stacks during infection.


E. Ronzone, J Wesolowski, Laura D. Bauler, Anshul Bhardwaj, Ted Hackstadt, F. Paumet (2014)An alpha-helical core encodes the dual functions of the chlamydial protein IncA” Journal of Biological Chemistry, 289

Here, the functional core of the SNARE-like protein IncA has been identified, which provides the basis for a more comprehensive understanding of its mechanisms of action and could aid in the development of novel therapeutics capable of interfering with its pathogenic function in vivo. This project provides the most detailed understanding of how a chlamydial inclusion protein operates to manipulate membrane fusion.


J. Wesolowski, F. Paumet (2014) Escherichia coli exposure inhibits exocytic SNARE-mediated membrane fusion in mast cellsTraffic 15:516-530

This study demonstrates that E. coli exposure inhibits the formation of the exocytic SNARE complex and thus the release of granules. As a result, IgE-induced inflammatory reactions are significantly dampened. Ultimately, these results suggest that the microenvironment within which mast cells reside modulates their activation.


E. Ronzone, F. Paumet (2013)Two coiled-coil domains of Chlamydia trachomatis IncA affect membrane fusion events during infectionPLoS One 8:e69769

These results demonstrate for the first time that Chlamydia employs SNARE-like virulence factors that positively and negatively affect membrane fusion and promote infection.


Recent Publications

Chlamydia hijacks ARF GTPases to coordinate microtubule posttranslational modifications and golgi complex positioning

Taking control: Reorganization of the host cytoskeleton by Chlamydia

A functional core of IncA is required for Chlamydia trachomatis inclusion fusion

An α-helical core encodes the dual functions of the chlamydial protein IncA

Escherichia coli exposure inhibits exocytic SNARE-mediated membrane fusion in mast cells

Extracellular traps are associated with human and mouse neutrophil and macrophage mediated killing of larval Strongyloides stercoralis

Two Coiled-Coil Domains of Chlamydia trachomatis IncA Affect Membrane Fusion Events during Infection

A Novel Function for SNAP29 (Synaptosomal-Associated Protein of 29 kDa) in Mast Cell Phagocytosis

The impact of bacterial infection on mast cell degranulation

SNARE motif: A common motif used by pathogens to manipulate membrane fusion

Intracellular bacteria encode inhibitory SNARE-like proteins

SNARE protein mimicry by an intracellular bacterium

Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins

Concerted auto-regulation in yeast endosomal t-SNAREs

The specificity of SNARE-dependent fusion encoded in the SNARE motif

i-SNAREs: Inhibitory SNAREs that fine-tune the specificity of membrane fusion

Cell fusion | La fusion cellulaire

SNAREs and associated regulators in the control of exocytosis in the RBL-2H3 mast cell line

Mechanisms of membrane fusion | Mécanisme de la fusion membranaire

A t-SNARE of the endocytic pathway must be activated for fusion