| RRC ID |
68513
|
| 著者 |
Cantarelli VV, Takahashi A, Yanagihara I, Akeda Y, Imura K, Kodama T, Kono G, Sato Y, Honda T.
|
| タイトル |
Talin, a host cell protein, interacts directly with the translocated intimin receptor, Tir, of enteropathogenic Escherichia coli, and is essential for pedestal formation.
|
| ジャーナル |
Cell Microbiol
|
| Abstract |
Enteropathogenic Escherichia coli (EPEC) is able to inject its own receptor, a transmembrane protein called translocated intimin receptor, Tir, into the host epithelial cell. The bacterium then uses an outer membrane protein, intimin, to bind to Tir and remains firmly attached to the host cell surface for the duration of the infection. The bacterium is also able to trigger the rearrangement of several host cell proteins, culminating with the formation of an actin-rich, pedestal-like structure beneath the EPEC adherence site. Although several cytoskeletal proteins are rearranged following EPEC infection, the exact role played by these proteins during pedestal formation remains unknown. We report here that talin, an integrin-binding protein, is recruited by EPEC and associates directly with Tir. By surface plasmon resonance (SPR), the predicted value for the dissociation constant (KD) for Tir-talin binding was 1.86 x 10(-7) M. We also demonstrate that microinjection of anti-talin antibodies into HeLa cells resulted in the complete inability to focus actin filaments beneath the attached bacterium. These findings demonstrate that talin is essential for EPEC-induced pedestal formation in infected cells.
|
| 巻・号 |
3(11)
|
| ページ |
745-51
|
| 公開日 |
2001-11-1
|
| DOI |
10.1046/j.1462-5822.2001.00156.x
|
| PII |
156
|
| PMID |
11696034
|
| MeSH |
Actins / metabolism
Escherichia coli / pathogenicity*
Escherichia coli / physiology*
Escherichia coli Infections / microbiology
Escherichia coli Proteins*
HeLa Cells
Humans
Protein Binding
Receptors, Cell Surface / metabolism*
Surface Plasmon Resonance
Talin / metabolism*
Virulence
|
| IF |
3.43
|
| リソース情報 |
| ヒト・動物細胞 |
HeLa(RCB0007) |
