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Titolo:
A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association
Autore:
Dersch, P; Isberg, RR;
Indirizzi:
Tufts Univ, Sch Med, Dept Mol Biol & Microbiol, Boston, MA 02111 USA TuftsUniv Boston MA USA 02111 Mol Biol & Microbiol, Boston, MA 02111 USA Howard Hughes Med Inst, Boston, MA 02111 USA Howard Hughes Med Inst Boston MA USA 02111 Med Inst, Boston, MA 02111 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 5, volume: 18, anno: 1999,
pagine: 1199 - 1213
SICI:
0261-4189(19990301)18:5<1199:AROTYP>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
OUTER-MEMBRANE PROTEIN; ESCHERICHIA-COLI; BINDING DOMAIN; BACTERIAL INTERNALIZATION; CELLULAR INTERNALIZATION; CITROBACTER-FREUNDII; SIGNAL-TRANSDUCTION; GENETIC-LOCUS; INV GENE; ENTEROCOLITICA;
Keywords:
bacterial uptake; integrin receptor clustering; invasin; protein-protein interaction; Yersinia pseudotuberculosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Isberg, RR TuftsAUniv, Sch Med, Dept Mol Biol & Microbiol, 136 Harrison Ave, Boston, M Tufts Univ 136 Harrison Ave Boston MA USA 02111 Ave, Boston, M
Citazione:
P. Dersch e R.R. Isberg, "A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association", EMBO J, 18(5), 1999, pp. 1199-1213

Abstract

Invasin allows efficient entry into mammalian cells by Yersinia pseudotuberculosis. It has been shown that the C-terminal 192 amino acids of invasin are essential for binding of beta(1) integrin receptors and subsequent uptake. By analyzing the internalization of latex beads coated with invasin derivatives, an additional domain of invasin was shown to be required for efficient bacterial internalization, A monomeric derivative encompassing the C-terminal 197 amino acids was inefficient at promoting entry of latex beads,whereas dimerization of this derivative by antibody significantly increased uptake. By using the DNA-binding domain of lambda repressor as a reporterfor invasin self-interaction, we have demonstrated that a region of the invasin protein located N-terminal to the cell adhesion domain of invasin is able to self-associate. Chemical crosslinking studies of purified and surface-exposed invasin proteins, and the dominant-interfering effect of a nonfunctional invasin derivative are consistent with the presence of a self-association domain that is located within the region of invasin that enhances bacterial uptake, We conclude that interaction of homomultimeric invasin with multiple integrins establishes tight adherence and receptor clustering, thus providing a signal for internalization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 04:04:58