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Titolo:
In vitro binding characteristics and affinity for sulfatide of Escherichiacoli STb enterotoxin
Autore:
Beausoleil, HE; Dubreuil, JD;
Indirizzi:
Univ Montreal, Fac Med Vet, Dept Pathol & Microbiol, GREMIP, St Hyacinthe,PQ J2S 7C6, Canada Univ Montreal St Hyacinthe PQ Canada J2S 7C6 Hyacinthe,PQ J2S 7C6, Canada
Titolo Testata:
RECEPTORS & CHANNELS
fascicolo: 5, volume: 7, anno: 2001,
pagine: 401 - 411
SICI:
1060-6823(2001)7:5<401:IVBCAA>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTESTINAL SECRETORY ACTION; B STB; CELL SURFACE; PIG JEJUNUM; TOXIN STB; PROTEIN; ADHESION; MEMBRANE; GLYCOSPHINGOLIPIDS; IDENTIFICATION;
Keywords:
Escherichia coli; heat-stable enterotoxin b; receptor; sulfatide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Dubreuil, JD Univ Montreal, Fac Med Vet, Dept Pathol & Microbiol, GREMIP, 3200 Sicotte,POB 5000, St Hyacinthe, PQ J2S 7C6, Canada Univ Montreal 3200 Sicotte,POB 5000 St Hyacinthe PQ Canada J2S 7C6
Citazione:
H.E. Beausoleil e J.D. Dubreuil, "In vitro binding characteristics and affinity for sulfatide of Escherichiacoli STb enterotoxin", RECEPT CHAN, 7(5), 2001, pp. 401-411

Abstract

It has previously been demonstrated that sulfatide (3 ' -sulfogalactosyl-ceramide), present at the surface of epithelial cells of the small intestineof pigs, interacts with the thermostable enterotoxin b (STb) produced by ETEC, and that this molecule is implicated in the mechanism of action of thetoxin. However, few things are known about the affinity and physical characteristics of the interaction between these two macromolecules. In this study, using a microtiter plate binding assay (MPBA), we showed that STb toxinhas a strong specificity for sulfatide and that this binding is dose-dependent and saturable. A very weak binding occurred with galactosyl-ceramide whereas attachment to 3 ' -sulfolactosyl-ceramide corresponded to 76% of thebinding to sulfatide. STb toxin was shown to possess a lectin-like property; a significative binding was observed when a terminal beta -galactose waspresent in the glycosphingolipids tested and an increased binding was observed in presence of a sulfate group in position 3 on the galactose. These findings suggest that a sulfated galactosyl residue seems to represent the epitope recognized by the toxin. The reaction between sulfatide and STb toxin is also time and temperature dependent and is not affected by pH. The interaction was not inhibited by free sugars, sulfated polymers, glycolipids or free ions, but was partly inhibited by high concentrations of charged sugars. STb-sulfatide binding process is a low affinity interaction, as demonstrated by the determined K-d of 2-6 +/- 1,5 muM.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/05/20 alle ore 14:52:42