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Multi-antennary Galβ1→4GlcNAc and Galβ1→3GalNAc clusters as important ligands for a lectin isolated from the spongeGeodia cydonium

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
427
Issue
1
Identifiers
DOI: 10.1016/s0014-5793(98)00411-6
Keywords
  • Lectin Binding Property
  • Geodia Cydoniumlectin I
  • Multi-Antennary Galβ1→4Glcnac
  • Galβ1→3Galnac Cluster
Disciplines
  • Biology

Abstract

Abstract The affinity of a lectin from the sponge Geodia cydonium (GCL-I) for multi-antennary Galβ1→4GlcNAc and Galβ1→3GalNAc ligands was studied by both the biotin/avidin-based microtiter plate lectin binding assay and the inhibition of lectin-glycoform interaction. Among the glycoforms tested for binding, GCL-I reacted strongly with three multi-antennary Galβ1→4GlcNAc clusters containing glycoproteins (asialo human and bovine α 1-acid gps and asialo fetuin), T (Galβ1→3GalNAc) rich glycoprotein from porcine salivary gland, asialo bird nest gp, and human blood group A active cyst gp, while human and bovine α 1-acid gps, fetuin, and Tn containing gps were inactive. Among the haptens tested for inhibition, tri-antennary Galβ1→4GlcNAc (Tri-II) was about 1500, 72, and 72 times more active than GalNAc, Galβ1→4GlcNAc (II), and Galβ1→3GalNAc (T), respectively. Based on the present and previous results, it is proposed that tri-antennary Galβ1→4GlcNAc and Galβ1→3GalNAc clusters, in addition to GalNAcα1→3GalNAc and GalNAcα1→3Gal, are also important ligands for binding; and sialic acid of glycoprotein does interfere with binding.

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