Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC).

@article{Huang2002HostFA,
  title={Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC).},
  author={Lily Huang and Balraj Mittal and Joseph W Sanger and Jean M. Sanger},
  journal={Cell motility and the cytoskeleton},
  year={2002},
  volume={52 4},
  pages={
          255-65
        }
}
Enteropathogenic Escherichia coli (EPEC) attach to the plasma membrane of infected host cells and induce diarrhea in a variety of farm animals as well in humans. These bacteria inject a three-domain protein receptor, Tir (translocated intimin receptor), that is subsequently inserted into the plasma membrane. EPEC induce the host cell to form membrane-covered actin-rich columns called pedestals. Focal adhesion constituents, alpha-actinin, talin, and vinculin, are localized along the length of… 
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Host protein interactions with enteropathogenic Escherichia coli (EPEC): 14‐3‐3τ binds Tir and has a role in EPEC‐induced actin polymerization
TLDR
This study indicates a direct functional role for the 14‐3‐3τ:Tir interaction and is the first to demonstrate the association of a host protein with the surface of EPEC.
Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7.
Actin Pedestal Formation on Mammalian Cells by Enteropathogenic Escherichia coli : A Dissertation
TLDR
This work has shown that EPEC and EHEC Tir are not functionally interchangeable, and that pedestals are formed independently of Nck, and require translocation of bacterial factors in addition to Tir to trigger actin signaling.
Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly
TLDR
It is found that the COOH terminus of Tir, by itself, is sufficient to initiate a complete signaling cascade leading to pedestal formation, and clustering of Nck by a 12-residue Tir phosphopeptide triggered actin tail formation in Xenopus egg extracts.
Dynamin is required for F‐actin assembly and pedestal formation by enteropathogenic Escherichia coli (EPEC)
TLDR
This study found that in HeLa cells, both endogenous and overexpressed Dyn2 were recruited to sites of EPEC attachment, indicating that Dyn2 is an integral component of the signalling cascade leading to actin polymerization in EPEC pedestals.
Adhesion of enteropathogenic Escherichia coli to host cells
Enteropathogenic Escherichia coli (EPEC) adhere to the intestinal mucosa and to tissue culture cells in a distinctive fashion, destroying microvilli, altering the cytoskeleton and attaching…
Involvement of the intermediate filament protein cytokeratin‐18 in actin pedestal formation during EPEC infection
TLDR
This study is the first to implicate intermediate filaments in microfilament reorganization following EPEC infection and identifies cytokeratin 18 as a novel Tir partner protein.
Actin and alpha-actinin dynamics in the adhesion and motility of EPEC and EHEC on host cells.
TLDR
A simple physical model was developed to describe elongation and translocation of EPEC/EHEC pedestals in terms of actin polymerization and depolymerization dynamics.
The basolateral vesicle sorting machinery and basolateral proteins are recruited to the site of enteropathogenic E. coli microcolony growth at the apical membrane
TLDR
In addition to disrupting host cell fence function, local host cell plasma membrane protein composition is changed by altered protein trafficking and recruitment of basolateral proteins to the apical microcolony.
Dual infection system identifies a crucial role for PKA‐mediated serine phosphorylation of the EPEC‐Tir‐injected effector protein in regulating Rac1 function
TLDR
The co‐infection approach is a powerful strategy for defining novel effector function with important implications for characterizing mechanisms and regulatory signalling pathways in bacterial pathogenesis.
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References

SHOWING 1-10 OF 43 REFERENCES
Interaction of the enteropathogenic Escherichia coli protein, translocated intimin receptor (Tir), with focal adhesion proteins.
TLDR
These experiments support a model in which the cytoplasmic domains of Tir recruit a number of focal adhesion proteins that can bind actin filaments to form pedestals.
Talin, a host cell protein, interacts directly with the translocated intimin receptor, Tir, of enteropathogenic Escherichia coli, and is essential for pedestal formation
TLDR
It is demonstrated that talin is essential for EPEC‐induced pedestal formation in infected cells, and microinjection of anti‐talin antibodies into HeLa cells resulted in the complete inability to focus actin filaments beneath the attached bacterium.
Identification of the intimin‐binding domain of Tir of enteropathogenic Escherichia coli
TLDR
It is confirmed that Tir–intimin interactions are needed for cytoskeletal organization and predicted topology for Tir is supported, with both N‐ and C‐terminal regions in the mammalian cell cytosol.
Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with α-actinin
Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin.
TLDR
It is shown that Tir directly binds the cytoskeletal protein alpha-actinin, the first known direct linkage between extracellular EPEC, through the transmembrane protein Tir, to the host cell actin cytoskeleton via alpha- actinin.
Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells
TLDR
It is shown that tyrosine 474 of Tir directly binds the host-cell adaptor protein Nck, and that Nck is required for the recruitment of both neural Wiskott–Aldrich-syndrome protein (N-WASP) and the actin-related protein (Arp)2/3 complex to the EPEC pedestal, directly linking Tir to the cytoskeleton.
Recruitment of Cytoskeletal and Signaling Proteins to Enteropathogenic and Enterohemorrhagic Escherichia coli Pedestals
TLDR
It is demonstrated that although EPEC and EHEC recruit similar cytoskeletal proteins, there are also significant differences in pedestal composition.
Crystal structure of enteropathogenic Escherichia coli intimin–receptor complex
TLDR
The crystal structures of an EPEC intimin carboxy-terminal fragment alone and in complex with the EPEC Tir intimin-binding domain are described, giving insight into the molecular mechanisms of adhesion of A/E pathogens.
Role of Tir and Intimin in the Virulence of Rabbit Enteropathogenic Escherichia coli Serotype O103:H2
TLDR
The role of intimin and its translocated coreceptor (Tir) in the pathogenicity of REPEC has been confirmed and it is shown, for the first time, that Tir is also a key factor in vivo for pathogenicicity.
Enteropathogenic Escherichia coli (EPEC) attachment to epithelial cells: exploiting the host cell cytoskeleton from the outside
TLDR
Studies of EPEC‐induced cytoskeletal rearrangements have begun to provide clues as to the mechanisms used by this pathogen to subvert the host cell cytoskeleton and signalling pathways, and have shed new light on how EPEC might cause diarrhoea.
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