Binding of class II Escherichia coli enterotoxins to mouse Y1 and intestinal cells.
The binding of class II Escherichia coli heat-labile enterotoxins (LT) to Y1 tissue-cultured cells and mouse intestinal cells was studied and compared with that of class I toxins, including cholera enterotoxin. All radioiodinated (125I) toxins retained their biological activities in both model systems, but only LTIIb could be shown to bind specifically to target cells. LTIIa could inhibit the binding of both class I and LTIIb toxins, a finding which correlates with its ability to bind to multiple gangliosides. LTIIb could not inhibit the binding of the other enterotoxins. The binding and activity of class II toxins could not be modulated by prior exposure of target cells to the B subunit of LTI.
Donta
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University of Connecticut Health Center, Farmington 06032.
Tomicic
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Holmes
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D000311:Adrenal Glands / Q000378:metabolism*; D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism*; D002478:Cells, Cultured; D002772:Cholera Toxin / Q000378:metabolism; D046508:Culture Techniques; D004306:Dose-Response Relationship, Immunologic; D004768:Enterotoxins / Q000378:metabolism*; D004926:Escherichia coli / Q000472:pathogenicity*; D029968:Escherichia coli Proteins; D006162:Guanylate Cyclase; D007413:Intestinal Mucosa / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D011956:Receptors, Cell Surface / Q000378:metabolism; D000074261:Receptors, Enterotoxin; D050705:Receptors, Guanylate Cyclase-Coupled; D018000:Receptors, Peptide; D013997:Time Factors
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D011956:Receptors, Cell Surface; D018000:Receptors, Peptide; D002772:Cholera Toxin; C027538:heat-labile enterotoxin, E coli; D006162:Guanylate Cyclase; D000074261:Receptors, Enterotoxin; D050705:Receptors, Guanylate Cyclase-Coupled