Home > Publications database > The EHEC-host interactome reveals novel targets for the translocated intimin receptor. > print |
001 | 119665 | ||
005 | 20240228134948.0 | ||
024 | 7 | _ | |a 10.1038/srep07531 |2 doi |
024 | 7 | _ | |a pmid:25519916 |2 pmid |
024 | 7 | _ | |a pmc:PMC4269881 |2 pmc |
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037 | _ | _ | |a DKFZ-2017-00296 |
041 | _ | _ | |a eng |
082 | _ | _ | |a 000 |
100 | 1 | _ | |a Blasche, Sonja |0 P:(DE-HGF)0 |b 0 |e First author |
245 | _ | _ | |a The EHEC-host interactome reveals novel targets for the translocated intimin receptor. |
260 | _ | _ | |a London |c 2014 |b Nature Publishing Group |
336 | 7 | _ | |a article |2 DRIVER |
336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1520587178_3333 |2 PUB:(DE-HGF) |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
520 | _ | _ | |a 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 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. |
536 | _ | _ | |a 312 - Functional and structural genomics (POF3-312) |0 G:(DE-HGF)POF3-312 |c POF3-312 |f POF III |x 0 |
588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
650 | _ | 7 | |a Adhesins, Bacterial |2 NLM Chemicals |
650 | _ | 7 | |a Escherichia coli Proteins |2 NLM Chemicals |
650 | _ | 7 | |a EspJ protein, E coli |2 NLM Chemicals |
650 | _ | 7 | |a HPCAL1 protein, human |2 NLM Chemicals |
650 | _ | 7 | |a NCALD protein, human |2 NLM Chemicals |
650 | _ | 7 | |a Neurocalcin |2 NLM Chemicals |
650 | _ | 7 | |a Receptors, Cell Surface |2 NLM Chemicals |
650 | _ | 7 | |a Tir protein, E coli |2 NLM Chemicals |
650 | _ | 7 | |a Transcription Factors |2 NLM Chemicals |
650 | _ | 7 | |a eaeA protein, E coli |0 147094-99-3 |2 NLM Chemicals |
650 | _ | 7 | |a Protein-Serine-Threonine Kinases |0 EC 2.7.11.1 |2 NLM Chemicals |
650 | _ | 7 | |a STK16 protein, human |0 EC 2.7.11.1 |2 NLM Chemicals |
700 | 1 | _ | |a Arens, Stefan |b 1 |
700 | 1 | _ | |a Ceol, Arnaud |b 2 |
700 | 1 | _ | |a Siszler, Gabriella |0 P:(DE-HGF)0 |b 3 |
700 | 1 | _ | |a Schmidt, M Alexander |b 4 |
700 | 1 | _ | |a Häuser, Roman |0 P:(DE-HGF)0 |b 5 |
700 | 1 | _ | |a Schwarz, Frank |0 P:(DE-He78)16e91871b8403eb9e93080b2ff38c0a2 |b 6 |u dkfz |
700 | 1 | _ | |a Wuchty, Stefan |b 7 |
700 | 1 | _ | |a Aloy, Patrick |b 8 |
700 | 1 | _ | |a Uetz, Peter |b 9 |
700 | 1 | _ | |a Stradal, Theresia |b 10 |
700 | 1 | _ | |a Koegl, Manfred |0 P:(DE-HGF)0 |b 11 |e Last author |
773 | _ | _ | |a 10.1038/srep07531 |g Vol. 4, p. 7531 - |0 PERI:(DE-600)2615211-3 |p 7531 - |t Scientific reports |v 4 |y 2014 |x 2045-2322 |
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