The EHEC-host interactome reveals novel targets for the translocated intimin receptor.
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Schmidt, M Alexander
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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.
CitationThe EHEC-host interactome reveals novel targets for the translocated intimin receptor. 2014, 4:7531 Sci Rep
AffiliationHelmholtz Centre for infection research; Inhooffenstr. 7; D-38124 Braunschweig; Germany.
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- Characterization of the binding surface of the translocated intimin receptor, an essential protein for EPEC and EHEC cell adhesion.
- Authors: Ross NT, Miller BL
- Issue date: 2007 Dec
- Enterohemorrhagic Escherichia coli O157:H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated.
- Authors: DeVinney R, Stein M, Reinscheid D, Abe A, Ruschkowski S, Finlay BB
- Issue date: 1999 May
- Crystal structure of EHEC intimin: insights into the complementarity between EPEC and EHEC.
- Authors: Yi Y, Ma Y, Gao F, Mao X, Peng H, Feng Y, Fan Z, Wang G, Guo G, Yan J, Zeng H, Zou Q, Gao GF
- Issue date: 2010 Dec 16
- Nck adaptors, besides promoting N-WASP mediated actin-nucleation activity at pedestals, influence the cellular levels of enteropathogenic Escherichia coli Tir effector.
- Authors: Nieto-Pelegrin E, Kenny B, Martinez-Quiles N
- Issue date: 2014
- EspZ of enteropathogenic and enterohemorrhagic Escherichia coli regulates type III secretion system protein translocation.
- Authors: Berger CN, Crepin VF, Baruch K, Mousnier A, Rosenshine I, Frankel G
- Issue date: 2012