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  • Title: Analysis of receptor-binding site in Escherichia coli enterotoxin.
    Author: Tsuji T, Honda T, Miwatani T, Wakabayashi S, Matsubara H.
    Journal: J Biol Chem; 1985 Jul 15; 260(14):8552-8. PubMed ID: 3924916.
    Abstract:
    Heat-labile enterotoxin produced by enterotoxigenic Escherichia coli and cholera enterotoxin are both composed of A and B subunits. The A subunit is an enzymatically active ADP-ribosylating subunit, while the B subunit, consisting of 103 amino acids, binds the toxin to a receptor, GM1-ganglioside, on the cell surface. A mutant isolated after treatment of E. coli producing heat-labile enterotoxin with N-methyl-N'-nitro-N-nitrosoguanidine produces a B subunit that is unable to bind to ganglioside. This subunit was purified and its primary amino acid sequence was determined. It differed from the native B subunit in only one amino acid at position 33; namely it had aspartate instead of glycine at position 33 from the N terminus. Thus glycine at position 33 from the N terminus of the B subunit is important for binding the B subunit to the ganglioside receptor.
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