The amino acids ofEscherichia colienterotoxin B subunit involved in binding to Bio-Gel A-5m or to the glycoprotein from mouse intestinal epithelial cells
Copyright policy )The amino acids ofEscherichia colienterotoxin B subunit involved in binding to Bio-Gel A-5m or to the glycoprotein from mouse intestinal epithelial cells
We determined whether Arg13, Met31, and Ser95 of the heat-labile enterotoxin B subunit (LT-B) might be involved in Lt-B binding to oligosaccharides, which did not bind to the B subunit of the cholera toxin (CT-B). Three LT-B mutants, R13H, M31L, and S95A were prepared by substituting three amino acid residues that differ in CT-B. These mutants formed a pentamer and exhibited the same binding ability to the GM1ganglioside as native LT-B. Although these mutants did not bind to Bio-Gel A-5m, they did bind to the glycoprotein from mouse intestinal cells in the order R13H > M31L > S95A. These data suggest that Ser95, Met31, and Arg13 are important for LT-B binding to Bio-Gel A-5m, and that although Ser95 is also partially responsible for LT-B binding to the glycoprotein, Arg13 has no significant involvement in it.Key words: heat-labile enterotoxin, cholera toxin, Bio-Gel A-5m, glycoprotein.
- Fujita Health University Japan
Oligosaccharides, Epithelial Cells, Epithelium, Intestines, Enterotoxins, Mice, Escherichia coli, Mutagenesis, Site-Directed, Animals, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing, Gels, Cells, Cultured, Glycoproteins, Plasmids, Protein Binding
Oligosaccharides, Epithelial Cells, Epithelium, Intestines, Enterotoxins, Mice, Escherichia coli, Mutagenesis, Site-Directed, Animals, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing, Gels, Cells, Cultured, Glycoproteins, Plasmids, Protein Binding
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