Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Intimin from Shiga toxin-producing Escherichia coli and its isolated C-terminal domain exhibit different binding properties for Tir and a eukaryotic surface receptor
Autore:
Deibel, C; Dersch, P; Ebel, F;
Indirizzi:
Univ Giessen, Inst Med Mikrobiol, Giessen, Germany Univ Giessen Giessen Germany ssen, Inst Med Mikrobiol, Giessen, Germany Free Univ Berlin, Inst Mikrobiol, D-1000 Berlin, Germany Free Univ BerlinBerlin Germany D-1000 Mikrobiol, D-1000 Berlin, Germany Inst Pasteur, Unite Genet Mol, Paris, France Inst Pasteur Paris FranceInst Pasteur, Unite Genet Mol, Paris, France
Titolo Testata:
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY
fascicolo: 8, volume: 290, anno: 2001,
pagine: 683 - 691
SICI:
1438-4221(200103)290:8<683:IFSTEC>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOTUBERCULOSIS INVASIN PROTEIN; MAMMALIAN-CELLS; HOST-CELLS; ACTIN CONDENSATION; EPITHELIAL-CELLS; GENETIC-LOCUS; INTEGRINS; IDENTIFICATION; ATTACHMENT; EXPRESSION;
Keywords:
intimin; Tir; STEC; attaching and effacing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Ebel, F Max Von Pettenkofer Inst, Pettenkofer Str 9A, D-80336 Munich, Germany Max Von Pettenkofer Inst Pettenkofer Str 9A Munich Germany D-80336
Citazione:
C. Deibel et al., "Intimin from Shiga toxin-producing Escherichia coli and its isolated C-terminal domain exhibit different binding properties for Tir and a eukaryotic surface receptor", INT J MED M, 290(8), 2001, pp. 683-691

Abstract

The outer membrane protein intimin plays a crucial role in the attaching and effacing process employed by different enteropathogens to colonize the epithelial surface of their hosts. In this study we have characterized the C-terminal binding domain of intimin from the Shiga toxin-producing Escherichia coli strain 413/89-1, that belongs to the beta -subtype of intimins. Wefound that a fusion of this domain to the maltose-binding protein binds efficiently to both the translocated intimin receptor (Tir) and the surface of uninfected eukaryotic host cells. In contrast, no such binding was observed with the full-length protein localized on the bacterial surface. As the C-terminal domain of intimin and the full-length protein differ in their binding activity, we suggest that the intimin binding domain might be controlled by the N-terminal portion of the molecule to prevent unproductive interactions with molecules in the lumen of the gut.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 10:33:47