Structure-Based Exploration of the Ganglioside GM1 Binding Sites ofEscherichia coliHeat-Labile Enterotoxin and Cholera Toxin for the Discovery of Receptor Antagonists†

Biochemistry ◽  
1999 ◽  
Vol 38 (18) ◽  
pp. 5684-5692 ◽  
Author(s):  
Wendy E. Minke ◽  
Claudia Roach ◽  
Wim G. J. Hol ◽  
Christophe L. M. J. Verlinde
Keyword(s):  
Cholera Toxin ◽  
Binding Sites ◽  
Ganglioside Gm1 ◽  
Receptor Antagonists

scholarly journals Characterization of the receptor for cholera toxin and Escherichia coli heat-labile toxin in rabbit intestinal brush borders

1986 ◽  
Vol 238 (2) ◽  
pp. 313-322 ◽  
Author(s):  
S L Griffiths ◽  
R A Finkelstein ◽  
D R Critchley
Keyword(s):  
Escherichia Coli ◽  
Cholera Toxin ◽  
Binding Sites ◽  
Cell Membranes ◽  
Ganglioside Gm1 ◽  
Neuraminidase Treatment ◽  
Toxin Binding ◽  
B Subunit ◽  
Heat Labile ◽  
Brush Borders

125I-labelled heat-labile toxin (from Escherichia coli) and 125I-labelled cholera toxin bound to immobilized ganglioside GM1 and Balb/c 3T3 cell membranes with identical specificities, i.e. each toxin inhibited binding of the other. Binding of both toxins to Balb/c 3T3 cell membranes was saturable, with 50% of maximal binding occurring at 0.3 nM for cholera toxin and 1.1 nM for heat-labile toxin, and the number of sites for each toxin was similar. The results suggest that both toxins recognize the same receptor, namely ganglioside GM1. In contrast, binding of 125I-heat-labile toxin to rabbit intestinal brush borders at 0 degree C was not inhibited by cholera toxin, although heat-labile toxin inhibited 125I-cholera toxin binding. In addition, there were 3-10-fold more binding sites for heat-labile toxin than for cholera toxin. At 37 degrees C cholera toxin, but more particularly its B-subunit, did significantly inhibit 125I-heat-labile toxin binding. Binding of 125I-cholera toxin was saturable, with 50% maximal of binding occurring at 1-2 nM, and was quantitatively inhibited by 10(-8) M unlabelled toxin or B-subunit. By contrast, binding of 125I-heat-labile toxin was non-saturable (up to 5 nM), and 2 × 10(-7) M unlabelled B-subunit was required to quantitatively inhibit binding. Neuraminidase treatment of brush borders increased 125I-cholera toxin but not heat-labile toxin binding. Extensive digestion of membranes with Streptomyces griseus proteinase or papain did not decrease the binding of either toxin. The additional binding sites for heat-labile toxin are not gangliosides. Thin-layer chromatograms of gangliosides which were overlayed with 125I-labelled toxins showed that binding of both toxins was largely restricted to ganglioside GM1. However, 125I-heat-labile toxin was able to bind to brush-border galactoproteins resolved by SDS/polyacrylamide-gel electrophoresis and transferred to nitrocellulose.

Interaction of ganglioside GM1 with the B subunit of cholera toxin modulates intracellular free calcium in sensory neurons

1992 ◽  
Vol 33 (3) ◽  
pp. 466-475 ◽  
Author(s):  
D. Milani ◽  
M.-C. Minozzi ◽  
L. Petrelli ◽  
D. Guidolin ◽  
S. D. Skaper ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Sensory Neurons ◽  
Intracellular Free Calcium ◽  
Free Calcium ◽  
Ganglioside Gm1 ◽  
B Subunit

scholarly journals Targeting Multiple Binding Sites on Cholera Toxin B with Glycomimetic Polymers Promotes the Formation of Protein–Polymer Aggregates

2020 ◽  
Vol 21 (12) ◽  
pp. 4878-4887
Author(s):  
Gyusaang Youn ◽  
Jakob Cervin ◽  
Xiaoxi Yu ◽  
Surita R. Bhatia ◽  
Ulf Yrlid ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Binding Sites ◽  
Toxin B ◽  
Cholera Toxin B ◽  
Protein Polymer ◽  
Polymer Aggregates ◽  
Multiple Binding Sites ◽  
Multiple Binding

Identification of cholera toxin-binding sites in the nucleus of intestinal epithelial cells

FEBS Letters ◽  
1989 ◽  
Vol 242 (2) ◽  
pp. 309-313 ◽  
Author(s):  
Marianne E. Parkinson ◽  
Colin G. Smith ◽  
Peter B. Garland ◽  
Simon van Heyningen
Keyword(s):  
Epithelial Cells ◽  
Cholera Toxin ◽  
Binding Sites ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Toxin Binding
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