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@article{So:2016:10.1074/jbc.M115.700930,
author = {So, EC and Schroeder, GN and Carson, D and Mattheis, C and Mousnier, A and Broncel, M and Tate, EW and Frankel, GM},
doi = {10.1074/jbc.M115.700930},
journal = {Journal of Biological Chemistry},
pages = {5832--5843},
title = {The Rab-binding profiles of bacterial virulence factors during infection},
url = {http://dx.doi.org/10.1074/jbc.M115.700930},
volume = {291},
year = {2016}
}
TY - JOUR
AB - Legionella pneumophila, the causativeagent of Legionnaire’s disease, uses its typeIV secretion system to translocate over 300effector proteins into host cells. Theseeffectors subvert host cell signalingpathways to ensure bacterial proliferation.Despite their importance for pathogenesis,the roles of most of the effectors are yet tobe characterized. Key to understanding thefunction of effectors is the identification ofhost proteins they bind during infection. Wepreviously developed a novel tandemaffinitypurification (TAP) approach usinghexahistidine and BirA-specificbiotinylation tags for isolating translocatedeffector complexes from infected cellswhose composition were subsequentlydeciphered by mass spectrometry. Here wefurther advanced the workflow for the TAPapproach and determined the infectiondependentinteractomes of the effectorsSidM and LidA, which were previouslyreported to promiscuously bind multiple RabGTPases in vitro. In this study we defined astringent subset of Rab GTPases targeted bySidM and LidA during infection, comprisingof Rab1A, 1B, 6 and 10; in addition, LidAtargets Rab14 and 18. Taken together, thisstudy illustrates the power of this approachto profile the intracellular interactomes ofbacterial effectors during infection
AU - So,EC
AU - Schroeder,GN
AU - Carson,D
AU - Mattheis,C
AU - Mousnier,A
AU - Broncel,M
AU - Tate,EW
AU - Frankel,GM
DO - 10.1074/jbc.M115.700930
EP - 5843
PY - 2016///
SN - 1083-351X
SP - 5832
TI - The Rab-binding profiles of bacterial virulence factors during infection
T2 - Journal of Biological Chemistry
UR - http://dx.doi.org/10.1074/jbc.M115.700930
UR - http://hdl.handle.net/10044/1/30375
VL - 291
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821