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The Immunochemistry of Antibodies Sharing Concanavalin A's Anti-Mannosyl Binding Specificity¹

From the Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109

Abstract

Procedures were developed for the synthesis of the disaccharide hapten, p-isothiocyanatophenyl 2-O--D-mannopyranosyl--D-mannopyranoside, and for its conjugation to hemocyanin. The synthetic carbohydrate: protein antigen was then emulsified in complete Freund's adjuvant and injected into the footpads of New Zealand White rabbits. A population of the resulting anti-conjugate antibodies displayed some binding properties analogous to concanavalin A, the carbohydrate-binding protein of the jack bean. The antisera weakly precipitated mannans from Saccharomyces rouxii, S. cerevisiae, and an -(1 3)-mannopyranosyl transferase-deficient mutant from Kluyveromyces lactis Y58a. These polysaccharides, possessing side chains containing terminal -(1 2)-mannobiosyl residues, produce strong precipitation reactions with concanavalin A. In addition, various saccharides were tested for their ability to inhibit the interaction of anti-conjugate antisera with -(1 2)-mannobiosyl-containing polymers. p-Nitrophenyl 2-O--D-mannopyranosyl--D-mannopyranoside showed a strong complementarity for the binding sites of both the anti-conjugate antisera and concanavalin A. However, the antibody failed to bind a concanavalin A-reactive mouse fibrosarcoma or to stimulate mitogenesis of human peripheral lymphocytes.

Footnotes

¹ This work was supported by National Institutes of Health Training Grant GM-00187 and United States Public Health Service Grant AM-10171.

² Present address: Laboratory of Pathology, National Institutes of Health, Bethesda, Maryland 20014.