Differential involvement of cell surface sialic acid residues in wheat germ agglutinin binding to parental and wheat germ agglutinin-resistant chinese hamster ovary cells

Pamela Stanley, Tadashi Sudo, Jeremy P. Carver

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56 Scopus citations

Abstract

Two Chinese hamster ovary (CHO) cell mutants selected for resistance to wheat germ agglutinin (WGA) have been shown to exhibit defective sialylation of membrane glycoproteins and a membrane glycolipid, GM3. The mutants (termed WgaRII and WgaRIII) have been previously shown to belong to different genetic complementation groups and to exhibit different WGA-binding abilities. These mutants and a WGA-resistant CHO cell mutant termed WgaRI (which also possesses a surface sialylation defect arising from a deficient iV-acetylglucosami-nyltransferase activity), have enabled us to investigate the role of sialic acid in WGA binding at the cell surface. Scatchard plots of the binding of 125I-WGA (1 ng/ml to 1 mg/ml) to parental and WgaR CHO cells before and after a brief treatment with neuraminidase provide evidence for several different groups of sialic acid residues at the CHO cell surface which may be distinguished by their differential involvement in WGA binding to CHO cells.

Original languageEnglish (US)
Pages (from-to)60-69
Number of pages10
JournalJournal of Cell Biology
Volume85
Issue number1
DOIs
StatePublished - Apr 1 1980

ASJC Scopus subject areas

  • Cell Biology

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