Imperial College London


Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Pathogenesis



+44 (0)20 7594 5253g.frankel




1.46Flowers buildingSouth Kensington Campus






BibTex format

author = {Furniss, RCD and Slater, S and Frankel, G and Clements, A},
doi = {10.1016/j.jmb.2016.05.023},
journal = {Journal of Molecular Biology},
pages = {3399--3407},
title = {Enterohaemorrhagic E. coli modulates an ARF6:Rab35 signalling axis to prevent recycling endosome maturation during infection},
url = {},
volume = {428},
year = {2016}

RIS format (EndNote, RefMan)

AB - Enteropathogenic and enterohaemorrhagic Escherichia coli (EPEC/EHEC) manipulate a plethora of host cell processes to establish infection of the gut mucosa. This manipulation is achieved via the injection of bacterial effector proteins into host cells using a Type III secretion system. We have previously reported that the conserved EHEC and EPEC effector EspG disrupts recycling endosome function, reducing cell surface levels of host receptors through accumulation of recycling cargo within the host cell. Here we report that EspG interacts specifically with the small GTPases ARF6 and Rab35 during infection. These interactions target EspG to endosomes and prevent Rab35-mediated recycling of cargo to the host cell surface. Furthermore, we show that EspG has no effect on Rab35-mediated uncoating of newly formed endosomes, and instead leads to the formation of enlarged EspG/TfR/Rab11 positive, EEA1/Clathrin negative stalled recycling structures. Thus, this paper provides a molecular framework to explain how EspG disrupts recycling whilst also reporting the first known simultaneous targeting of ARF6 and Rab35 by a bacterial pathogen.
AU - Furniss,RCD
AU - Slater,S
AU - Frankel,G
AU - Clements,A
DO - 10.1016/j.jmb.2016.05.023
EP - 3407
PY - 2016///
SN - 1089-8638
SP - 3399
TI - Enterohaemorrhagic E. coli modulates an ARF6:Rab35 signalling axis to prevent recycling endosome maturation during infection
T2 - Journal of Molecular Biology
UR -
UR -
VL - 428
ER -