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    Identification of two binding sites for wheat-germ agglutinin on polylactosamine-type oligosaccharides.

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    Authors
    Gallagher, John T
    Morris, Andrew J
    Dexter, T Michael
    Affiliation
    Cancer Research Campaign, Christie Hospital and Paterson Laboratories, Wilmslow Road, Manchester M20 9BX, UK.
    Issue Date
    1985-10-01
    
    Metadata
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    Abstract
    The carbohydrate-binding properties of wheat-germ agglutinin (WGA) have been studied by using glycopeptides isolated from the cell surfaces of a cultured murine myeloid cell line (416B). The glycopeptides were passed through affinity columns of lentil lectin (LCA), concanavalin A (Con A) and WGA arranged in series so that material reaching the WGA column had failed to bind to LCA or Con A. WGA-binding glycopeptides were step-eluted with 0.01 M, 0.1 M and 0.5 M-N-acetylglucosamine (GlcNAc), to yield weak (WGA-W), intermediate (WGA-I) and strong (WGA-S) affinity fractions. WGA-W and WGA-I contained 'N'- and 'O'-linked oligosaccharides bound to separate polypeptides. WGA-S consisted almost entirely of N-linked components. Our analytical work was concentrated mainly on the N-linked fractions. In these carbohydrates WGA affinity was directly proportional to molecular size but inversely related to N-acetylneuraminic acid content. The binding of the weak-affinity fraction was dependent on N-acetylneuraminic acid, but the intermediate- and strong-binding species interacted with the lectin by N-acetylneuraminic acid-independent mechanisms. N-linked glycopeptides in each WGA-binding class were almost totally degraded to monosaccharides by the concerted action of the exoglycosidases neuraminidase, beta-galactosidase and beta-N-acetylglucosaminidase. Treatment with endo-beta-galactosidase caused partial depolymerization, yielding some disaccharides but also a heterogeneous population of partially degraded components. These findings suggest that WGA binds with high affinity to internal GlcNAc residues in large oligosaccharides containing repeat sequences of Gal beta(1----4)GlcNAc beta(1----3) (i.e. polylactosamine-type glycans). N-Acetylneuraminic acid is involved only in low-affinity interactions with WGA. WGA therefore displays an intricate pattern of saccharide specificities that can be profitably utilized for structural analysis of complex carbohydrates.
    Citation
    Identification of two binding sites for wheat-germ agglutinin on polylactosamine-type oligosaccharides. 1985, 231 (1):115-22 Biochem J
    Journal
    The Biochemical Journal
    URI
    http://hdl.handle.net/10541/117106
    PubMed ID
    3840682
    Type
    Article
    Language
    en
    ISSN
    0264-6021
    Collections
    All Paterson Institute for Cancer Research

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