Interaction of a human blood group Sd(a−) Tamm‐Horsfall glycoprotein with applied lectins

FEBS Letters

Wu, June H.²  Chen, Chie-Pein¹  Watkins, Winifred M.³  Wu, Albert M.¹  Song, Shuh-Chyung¹ 

[1] Glyco-immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, Chang-Gung Medical College, Kwei-san, Tao-yuan, Taiwan;Department of Microbiology and Immunology, Glyco-immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, Chang-Gung Medical College, Kwei-san, Tao-yuan, Taiwan;Department of Haematology, Royal Postgraduate Medical School, DuCane Road, London W12 0NN, UK

关键词: Binding properties of applied lectins;    Native glycoprotein;    Asialo Tamm-Horsfall glycoprotein;    Gal;    d-galactopyranose;    Glc;    d-glucopyranose;    LFuc or Fuc;    l-fucopyranose;    GalNAc;    2-acetamido-2-deoxy-d-galactopyranose;    GlcNAc;    2-acetamido-2-deoxy-d-glucopyranose;    NeuAc;    N-acetyl-neuraminic acid;    THGP;    Tamm-Horsfall glycoprotein;    asialo THGP;    asialo Tamm-Horsfall glycoprotein;    II;    Galβ1 → 4GlcNAc;    L;    Galβ1 → 4Glc;   

DOI  :  10.1016/0014-5793(96)00320-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Unlike the human blood group Sd(a+) Tamm-Horsfall glycoprotein (THGP), the Sd(a−) one lacks terminal GalNAcβ1 → residues at the nonreducing ends. The binding properties of this glycoprotein and its asialo product with lectins were characterized by quantitative precipitin (QPA) and precipitin inhibition assays. Among 20 lectins tested by QPA, both native and asialo Sd(a−) THGP reacted best with Abrus precatorius and Ricinus communis and completely precipitated the lectin added. They also precipitated well Wistaria floribunda (WFA), Glycine max (SBA), Bauhinia purpurea alba, abrin-a and ricin, all of which recognize the Galβ1 → 4GlcNacβ1 → sequence, although at different strength. The lectin-glycan interactions were inhibited by Galβ1 → 4GlcNAc and Galβ1 → 4Glc. When the precipitability of Sd(a−) THGP was compared with that of the Sd(a+) phenotype, the native Sd(a−) THGP exhibited a 40% lesser affinity for WFA, SBA, WGA and mistletoe lectin-I (ML-I). Mapping the precipitation and inhibition profiles of the present study and the results of THGP Sd(a+), it is concluded that Sd(a−) THGP showed a strongly diminished affinity for GalNAcβ1 → active lectins (SBA and WFA) than the Sd(a+) phenotype.

【 授权许可】

Unknown