Recruitment and membrane interactions of host cell proteins during attachment of enteropathogenic and enterohaemorrhagic Escherichia coli.

The Biochemical Journal
Diana MuneraGad Frankel

Abstract

EPEC (enteropathogenic Escherichia coli) and EHEC (enterohaemorrhagic Escherichia coli) are attaching and effacing pathogens frequently associated with infectious diarrhoea. EPEC and EHEC use a T3SS (type III secretion system) to translocate effectors that subvert different cellular processes to sustain colonization and multiplication. The eukaryotic proteins NHERF2 (Na(+)/H(+) exchanger regulatory factor 2) and AnxA2 (annexin A2), which are involved in regulation of intestinal ion channels, are recruited to the bacterial attachment sites. Using a stable HeLa-NHERF2 cell line, we found partial co-localization of AnxA2 and NHERF2; in EPEC-infected cells, AnxA2 and NHERF2 were extensively recruited to the site of bacterial attachment. We confirmed that NHERF2 dimerizes and found that NHERF2 interacts with AnxA2. Moreover, we found that AnxA2 also binds both the N- and C-terminal domains of the bacterial effector Tir through its C-terminal domain. Immunofluorescence of HeLa cells infected with EPEC showed that AnxA2 is recruited to the site of bacterial attachment in a Tir-dependent manner, but independently of Tir-induced actin polymerization. Our results suggest that AnxA2 and NHERF2 form a scaffold complex that links adjacent T...Continue Reading

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Citations

Mar 26, 2016·Frontiers in Immunology·Julie Guignot, Guy Tran Van Nhieu
Dec 19, 2014·Scientific Reports·Sonja BlascheManfred Koegl
Aug 10, 2013·Cellular Microbiology·Yushuan LaiGad Frankel
Jul 2, 2016·Biological Chemistry·Alexander KuehnlUrsula Rescher
Mar 19, 2019·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Malik ZiboucheJesus Ayala-Sanmartin
Sep 29, 2018·ACS Applied Materials & Interfaces·Amitava MoulickVojtech Adam

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