Vitelline coat of Unio elongatulus: III. Glycan chain analysis of the 220- and 180-kD components by means of lectins

✍ Scribed by R. Focarelli; F. Leotta; R. Lampariello; Dr. Floriana Rosati

• Book ID: 102951624
• Publisher: John Wiley and Sons
• Year: 1995
• Tongue: English
• Weight: 594 KB
• Volume: 40
• Category: Article
• ISSN: 1040-452X
• DOI: 10.1002/mrd.1080400209

✦ Synopsis

Abstract

Lectins of different binding specificity were used to analyze the oligosaccharide chains of the 220‐ and 180‐kD proteins of the Unio elongatulus egg vitelline coat (vc). The lectins ConA and RCA~1~ reacted with both glycoproteins, and four other lectins reacted with one or other vc components. The lectin from Galanthus nivalis, which recognizes terminal mannose residues of N‐linked high mannose type oligosaccharide chains, bound specifically to the 180‐kD protein. Binding sites for this lectin were found throughout the vc of the differentiating oocyte and the mature egg. Lectins specific for the O‐linked oligosaccharide chains, such as AIA and PNA, reacted only with the 220‐kD protein species. Binding sites for these lectins were found only in the crater region. The presence of fucosyl residues on the glycan chains was investigated with lectins from Lotus tetragonolobus and Aleuria aurantia. The latter was positive on both glycoproteins, whereas LTA was only positive to the 220‐kD species. The binding sites of both these lectins were in the same areas as those of PNA and AIA. These results suggest that while the 180‐kD protein is part of the entire vc structure, the 220‐kD protein is prevalently accumulated in the crater region. Since this is where sperm recognition and interaction take place, it has been suggested the 220‐kD protein acts as a ligand molecule in the sperm‐egg interaction. © 1995 Wiley‐Liss, Inc.