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Titolo:
Enterohemorrhagic Escherichia coli O157 : H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated
Autore:
DeVinney, R; Stein, M; Reinscheid, D; Abe, A; Ruschkowski, S; Finlay, BB;
Indirizzi:
Univ British Columbia, Biotechnol Lab, Vancouver, BC V6T 1Z4, Canada Univ British Columbia Vancouver BC Canada V6T 1Z4 ver, BC V6T 1Z4, Canada
Titolo Testata:
INFECTION AND IMMUNITY
fascicolo: 5, volume: 67, anno: 1999,
pagine: 2389 - 2398
SICI:
0019-9567(199905)67:5<2389:EECO:H>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-TRANSDUCTION RESPONSES; EPITHELIAL-CELLS; INTIMATE ATTACHMENT; PROTEIN SECRETION; REQUIRES INTIMIN; BINDING DOMAIN; EAEA GENE; RABBIT; ESPA; TEMPERATURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Finlay, BB Univ British Columbia, Biotechnol Lab, Vancouver, BC V6T 1Z4, Canada Univ British Columbia Vancouver BC Canada V6T 1Z4 1Z4, Canada
Citazione:
R. DeVinney et al., "Enterohemorrhagic Escherichia coli O157 : H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated", INFEC IMMUN, 67(5), 1999, pp. 2389-2398

Abstract

Intimate attachment to the host cell leading to the formation of attachingand effacing (A/E) lesions is an essential feature of enterohemorrhagic Escherichia coli (EHEC) O157:H7 pathogenesis. In a related pathogen, enteropathogenic E. coli (EPEC), this activity is dependent upon translocation of the intimin receptor, Tir, which becomes tyrosine phosphorylated within the host cell membrane, In contrast, the accumulation of tyrosine-phosphorylated proteins beneath adherent EHEC bacteria does not occur, leading to questions about whether EHEC uses a Tir-based mechanism for adherence and A/E lesion formation. In this report, we demonstrate that EHEC produces a functional Tir that is inserted into host cell membranes, where it serves as an intimin receptor. However, unlike in EPEC, in EHEC Tir is not tyrosine phosphorylated yet plays a key role in both bacterial adherence to epithelial cells and pedestal formation. EHEC, but not EPEC, was unable to synthesize Tir in Luria-Bertani medium but was able to secrete Tir into M9 medium, suggesting that Tir synthesis and secretion may be regulated differently in these two pathogens. EHEC Tir and EPEC Tir both bind intimin and focus cytoskeletal rearrangements, indicating that tyrosine phosphorylation is not needed for pedestal formation. EHEC and EPEC intimins are functionally interchangeable, but EHEC Tir shows a much greater affinity for EHEC intimin than for EPEC intimin, These findings highlight some of the differences and similarities between EHEC and EPEC virulence mechanisms, which can be exploited to further define the molecular basis of pedestal formation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 05:04:15