Heterogeneity of intestinal receptors for Escherichia coli heat-stable enterotoxin
نویسندگان
چکیده
منابع مشابه
Enzyme-linked immunosorbent assay for Escherichia coli heat-stable enterotoxin.
The sensitivity of an enzyme-linked immunosorbent assay (ELISA) to detect pure native Escherichia coli heat-stable toxin (ST) and to identify ST-producing strains among clinical isolates was determined. Two synthetically produced ST preparations were used to raise hyperimmune antisera in rabbits and goats: ST(S), which has the same antigenicity as native ST; and ST(C), which is 15-fold more imm...
متن کاملProperties of synthetically produced Escherichia coli heat-stable enterotoxin.
The properties of a synthetically produced peptide composed of the same primary structure of 18 amino acids described for human Escherichia coli heat-stable enterotoxin were compared with those of purified heat-stable toxin obtained by bacterial growth. The dosage required to evoke fluid secretion in the suckling mouse and rat ligated ileal loop assays was the same for both toxins. The antigeni...
متن کاملBinding of Escherichia coli heat-stable enterotoxin to rat intestinal cells and brush border membranes.
The association of heat-stable enterotoxin (STa) produced by enterotoxigenic Escherichia coli 431 with isolated rat intestinal epithelial cells and brush border membranes was characterized. Specific binding of strain 431 125I-STa to a single class of specific high-affinity receptors was saturable and temperature dependent and reached a maximum between 5 and 10 min. A 1,000-fold excess of unlabe...
متن کاملInteraction of Escherichia coli heat-stable enterotoxin B with cultured human intestinal epithelial cells.
Binding of Escherichia coli heat-stable enterotoxin B (STb) to the human intestinal epithelial cell lines T84 and HT29 and to polarized T84 cells was studied to define the initial interaction of this peptide toxin with target cells. Equilibrium and competitive binding isotherms showed that 125I-STb bound specifically to T84 and HT29 cells; however, the toxin-epithelial cell interactions could b...
متن کاملProtection in rats immunized with Escherichia coli heat-stable enterotoxin.
Rats immunized with a semipurified preparation of the Escherichia coli heat-stable (ST) enterotoxin conjugated with a protein carrier were protected against challenge with semipurified or purified ST and viable organisms of multiple heterologous serotypes that produce only ST (LT-/ST+), but they were not protected against heal-labile (LT) toxin or viable strains which produce LT either alone (L...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1990
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.58.6.1817-1820.1990