Gary Schoolnik

Publication Details

  • Chemical and immunochemical studies on the receptor binding domain of cholera toxin B subunit. journal of biological chemistry Ludwig, D. S., Holmes, R. K., SCHOOLNIK, G. K. 1985; 260 (23): 12528-12534


    The contributions of various amino acids to the structure and function of cholera toxin B subunit were assessed with quantifiable, chemically conservative, reversible derivatizations, and sensitive assays of activity. A panel of monoclonal antibodies was employed to monitor the conformational integrity of modified protein and help distinguish the direct from indirect effects of chemical derivatization. We describe a novel monoclonal antibody, which competes with the receptor GM1 for binding to cholera toxin B subunit, and use this reagent to help identify critically located residues. Our data support the hypothesis that tryptophan participates directly in binding GM1. In addition, we propose a dual role for lysine: first, these basic residues maintain an electrostatic attraction vital to receptor recognition; second, at least 1 lysine resides near the receptor binding domain and may interact with GM1. The influence of arginyl and tyrosyl residues upon activity is re-examined. Finally, we present data which suggest, in variance with previous studies, that the intramolecular disulfide bond is vital to the structure and function of cholera toxin B subunit.

    View details for PubMedID 2413025

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