The EHEC-host interactome reveals novel targets for the translocated intimin receptor

Sonja Blasche, Stefan Arens, Arnaud Ceol, Gabriella Siszler, M. Alexander Schmid, Roman Häuser, Frank Schwarz, Stefan Wuchty, Patrick Aloy, Peter Uetz, Theresia Stradal, Manfred Koegl

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Enterohemorrhagic 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 thoseof 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.

Original languageEnglish (US)
Article number7531
JournalScientific reports
StatePublished - Dec 18 2014

ASJC Scopus subject areas

  • General


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