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dc.contributor.authorBlasche, Sonja
dc.contributor.authorArens, Stefan
dc.contributor.authorCeol, Arnaud
dc.contributor.authorSiszler, Gabriella
dc.contributor.authorSchmidt, M Alexander
dc.contributor.authorHäuser, Roman
dc.contributor.authorSchwarz, Frank
dc.contributor.authorWuchty, Stefan
dc.contributor.authorAloy, Patrick
dc.contributor.authorUetz, Peter
dc.contributor.authorStradal, Theresia
dc.contributor.authorKoegl, Manfred
dc.date.accessioned2015-01-19T15:02:33Z
dc.date.available2015-01-19T15:02:33Z
dc.date.issued2014
dc.identifier.citationThe EHEC-host interactome reveals novel targets for the translocated intimin receptor. 2014, 4:7531 Sci Repen
dc.identifier.issn2045-2322
dc.identifier.pmid25519916
dc.identifier.doi10.1038/srep07531
dc.identifier.urihttp://hdl.handle.net/10033/338555
dc.description.abstractEnterohemorrhagic E. coli (EHEC) manipulate their human host through at least 39 effector proteins which hijack host processes through direct protein-protein interactions (PPIs). To identify their protein targets in the host cells, we performed yeast two-hybrid screens, allowing us to find 48 high-confidence protein-protein interactions between 15 EHEC effectors and 47 human host proteins. In comparison to other bacteria and viruses we found that EHEC effectors bind more frequently to hub proteins as well as to proteins that participate in a higher number of protein complexes. The data set includes six new interactions that involve the translocated intimin receptor (TIR), namely HPCAL1, HPCAL4, NCALD, ARRB1, PDE6D, and STK16. We compared these TIR interactions in EHEC and enteropathogenic E. coli (EPEC) and found that five interactions were conserved. Notably, the conserved interactions included those of serine/threonine kinase 16 (STK16), hippocalcin-like 1 (HPCAL1) as well as neurocalcin-delta (NCALD). These proteins co-localize with the infection sites of EPEC. Furthermore, our results suggest putative functions of poorly characterized effectors (EspJ, EspY1). In particular, we observed that EspJ is connected to the microtubule system while EspY1 appears to be involved in apoptosis/cell cycle regulation.
dc.language.isoenen
dc.titleThe EHEC-host interactome reveals novel targets for the translocated intimin receptor.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research; Inhooffenstr. 7; D-38124 Braunschweig; Germany.en
dc.identifier.journalScientific reportsen
refterms.dateFOA2018-06-13T21:38:57Z
html.description.abstractEnterohemorrhagic E. coli (EHEC) manipulate their human host through at least 39 effector proteins which hijack host processes through direct protein-protein interactions (PPIs). To identify their protein targets in the host cells, we performed yeast two-hybrid screens, allowing us to find 48 high-confidence protein-protein interactions between 15 EHEC effectors and 47 human host proteins. In comparison to other bacteria and viruses we found that EHEC effectors bind more frequently to hub proteins as well as to proteins that participate in a higher number of protein complexes. The data set includes six new interactions that involve the translocated intimin receptor (TIR), namely HPCAL1, HPCAL4, NCALD, ARRB1, PDE6D, and STK16. We compared these TIR interactions in EHEC and enteropathogenic E. coli (EPEC) and found that five interactions were conserved. Notably, the conserved interactions included those of serine/threonine kinase 16 (STK16), hippocalcin-like 1 (HPCAL1) as well as neurocalcin-delta (NCALD). These proteins co-localize with the infection sites of EPEC. Furthermore, our results suggest putative functions of poorly characterized effectors (EspJ, EspY1). In particular, we observed that EspJ is connected to the microtubule system while EspY1 appears to be involved in apoptosis/cell cycle regulation.


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