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Human ZG16p recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system.

Abstract

Human zymogen granule protein 16 (ZG16p) contains a Jacalin-like lectin domain, although its glycan-binding properties are not fully understood. Here, we screened the glycan-binding specificity of ZG16p by recently developed glycoconjugate microarray. ZG16p appeared to exhibit selective binding to α- and β-linked mannose-polyacrylamide-biotin probes. In more quantitative analysis using frontal affinity chromatography, dissociation constants to two types of polyvalent mannose, i.e. high-density mannose and yeast mannan, were determined to be 1.3 and 1.7 µM, respectively. Mutation of the evolutionarily conserved amino acid Asp151, which is involved in sugar binding among the Jacalin-related lectins (JRLs), abolished binding activity to mannose. By immunohistochemical staining, ZG16p was specifically detected in mucus-secreting cells of the digestive system such as serosanguineous acinar cells of the parotid gland, acinar cells of the pancreas and goblet cells of the intestine. Finally, we showed that ZG16p recognizes pathogenic Candida and Malassezia species in a polyvalent mannose-dependent manner. We propose that ZG16p is a novel member of mannose-specific JRLs, which recognizes pathogenic fungi through non-self polyvalent mannose in the digestive system.

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  • Authors

    Tateno H, Yabe R, Sato T, Shibazaki A, Shikanai T, Gonoi T, Narimatsu H, Hirabayashi J

    Source

    Glycobiology 22:2 2012 Feb pg 210-20

    MeSH

    Binding Sites
    Candida
    Chromatography, Affinity
    Humans
    Intestines
    Lectins
    Malassezia
    Mannose
    Microarray Analysis
    Mutation
    Pancreas
    Parotid Gland
    Protein Structure, Tertiary
    Recombinant Proteins
    Tissue Distribution

    Pub Type(s)

    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    21893569