Structural studies on folding and interactions of glycoconjugates of immunological interests

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Sugar chains of glycoconjugates mediate molecular recognition involved in cell-cell communication and contribute to folding and quality control of glycoproteins. Although biological significance of sugar chains were widely recognized, little was known about their specific roles from a structural aspect. In the present study, we have developed nuclear magnetic resonance (NMR) and multi-dimensional HPLC methods for the elucidation of biological functions of sugar chains of glycoconjugates of immunological interests. By use of these techniques, we have addressed the following issues :1) Modes of interactions between sugar chains and intracellular lectins such as calreticulin and VIP-36.2) Roles of the sugar chains attached to the Fc portion of immunoglobulin G (IgG) in the interactions with Fcγ receptors and rheumatoid factors.3) NMR and HPLC analyses of the carbohydrate moieties expressed by recombinant CD1 glycoproteins.4) Glycosylation profiling of serum IgGs under a variety of pathological conditions.