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Titolo:
The enterohaemorrhagic Escherichia coli (serotype O157 : H7) Tir molecule is not functionally interchangeable for its enteropathogenic E-coli (serotype O127 : H6) homologue
Autore:
Kenny, B;
Indirizzi:
Univ Bristol, Sch Med Sci, Dept Pathol & Microbiol, Bristol BS8 1TD, Avon,England Univ Bristol Bristol Avon England BS8 1TD , Bristol BS8 1TD, Avon,England
Titolo Testata:
CELLULAR MICROBIOLOGY
fascicolo: 8, volume: 3, anno: 2001,
pagine: 499 - 510
SICI:
1462-5814(200108)3:8<499:TEEC(O>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSLOCATED INTIMIN RECEPTOR; HOST EPITHELIAL-CELLS; TYROSINE PHOSPHORYLATION; ENTEROCYTE EFFACEMENT; PROTEIN TRANSLOCATION; PATHOGENICITY ISLAND; SIGNAL-TRANSDUCTION; EFFACING PHENOTYPE; III SECRETION; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Kenny, B Univ Bristol, Sch Med Sci, Dept Pathol & Microbiol, Univ Walk, Bristol BS81TD, Avon, England Univ Bristol Univ Walk Bristol Avon England BS81TD Avon, England
Citazione:
B. Kenny, "The enterohaemorrhagic Escherichia coli (serotype O157 : H7) Tir molecule is not functionally interchangeable for its enteropathogenic E-coli (serotype O127 : H6) homologue", CELL MICROB, 3(8), 2001, pp. 499-510

Abstract

A major virulence determinant of enteropathogenic Escherichia coil (EPEC) is the Tir molecule that is translocated into the plasma membrane where it orchestrates cytoskeletal rearrangements. Tir undergoes several phosphorylation events within host cells, with modification on a tyrosine essential for its actin-nucleating function. The EHEC (serotype O157:H7) Tir homologue is not tyrosine phosphorylated implying that it uses an alternative mechanism to nucleate actin. This is supported in this study by the demonstration that EHEC Tir is unable to functionally substitute for its EPEC homologue. Like EPEC, the EHEC Tir molecule is phosphorylated within host cells, with the actin-nucleating dysfunction correlated to an altered modification profile. In contrast to EHEC Tir, the EPEC Tir molecule mediated actin nucleation whether delivered into host cells by either strain. Thus, it would appear that EHEC encodes specific factor(s) that facilitate the correct modification of its Tir molecule within host cells. Domain-swapping experiments revealed that the N-terminal, alpha -actinin binding, Tir domains were functionally interchangeable, with both the actin-nucleating dysfunction and altered modification profiles linked to the EHEC C-terminal Tir domain. This tyrosine-independent modification process presumably confers an advantage to EHEC O157:H7 and may contribute to the prevalence of this strain in EHEC disease. The presented data are also consistent with EPEC and EHEC sharing non-phosphotyrosine phosphorylation event(s), with an important role for such modifications in Tir function. An EHEC-induced phosphotyrosine dephosphorylation activity is also identified.

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Documento generato il 04/07/20 alle ore 22:45:57