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    Structure and binding analysis of Polyporus squamosus lectin in complex with the Neu5Acα2-6Galβ1-4GlcNAc human-type influenza receptor


    Kadirvelraj, Renuka and Grant, Oliver C. and Goldstein, Irwin J. and Winter, Harry C. and Tateno, Hiroaki and Fadda, Elisa and Woods, Robert J. (2011) Structure and binding analysis of Polyporus squamosus lectin in complex with the Neu5Acα2-6Galβ1-4GlcNAc human-type influenza receptor. Glycobiology, 21 (7). pp. 973-984. ISSN 0959-6658

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    Abstract

    Glycan chains that terminate in sialic acid (Neu5Ac) are frequently the receptors targeted by pathogens for initial adhesion. Carbohydrate-binding proteins (lectins) with specificity for Neu5Ac are particularly useful in the detection and isolation of sialylated glycoconjugates, such as those associated with pathogen adhesion as well as those characteristic of several diseases including cancer. Structural studies of lectins are essential in order to understand the origin of their specificity, which is particularly important when employing such reagents as diagnostic tools. Here, we report a crystallographic and molecular dynamics (MD) analysis of a lectin from Polyporus squamosus (PSL) that is specific for glycans terminating with the sequence Neu5Acα2-6Galβ. Because of its importance as a histological reagent, the PSL structure was solved (to 1.7 Å) in complex with a trisaccharide, whose sequence (Neu5Acα2-6Galβ1-4GlcNAc) is exploited by influenza A hemagglutinin for viral adhesion to human tissue. The structural data illuminate the origin of the high specificity of PSL for the Neu5Acα2-6Gal sequence. Theoretical binding free energies derived from the MD data confirm the key interactions identified crystallographically and provide additional insight into the relative contributions from each amino acid, as well as estimates of the importance of entropic and enthalpic contributions to binding.

    Item Type: Article
    Keywords: GLYCAM; PSL; influenza viral adhesion; lectin; molecular dynamics;
    Academic Unit: Faculty of Science and Engineering > Chemistry
    Item ID: 7735
    Identification Number: https://doi.org/10.1093/glycob/cwr030
    Depositing User: Elisa Fadda
    Date Deposited: 12 Jan 2017 12:11
    Journal or Publication Title: Glycobiology
    Publisher: Oxford University Press
    Refereed: Yes
    URI:

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