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Comparison of the carbohydrate moieties of recombinant soluble Fcε receptor (sFcε RII/sCD23) expressed inSaccharomyces cerevisiae and Chinese hamster ovary cells. Different O-glycosylation sites are used by yeast and mammalian cells

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Abstract

Recombinant human soluble low affinity receptor for the Fc portion of IgE (sFcεRII/sCD23) was produced inSaccharomyces cerevisiae or Chinese hamster ovary cells and subjected to carbohydrate analysis. Applied methods included analytical SDS-PAGE, reversed phase HPLC, methylation analysis and sequential degradation with exoglycosidases. The results revealed that sFcεRII derived from Chinese hamster ovary cells is glycosylated exclusively at Ser-147, containing mainly the trisaccharide Sia(α2–3)Gal(β1–3)GalNAc, whereas the yeast derived glycoprotein was glycosylated at Ser-167 and contained only α-mannosyl residues. It is shown here for the first time that different amino acids of a given protein can be O-glycosylated when expressed in yeast or Chinese hamster ovary cells.

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Authors and Affiliations

  1. Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria

    Inge Kalsner, Franz-Josef Schneider, Horst Ahorn & Ingrid Maurer-Fogy

  2. Biochemisches Institut am Klinikum der Universität Gieβen, FriedrichstraβE 24, W-6300, Gieβen, Germany

    Rudolf Geyer

Authors
  1. Inge Kalsner
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  2. Franz-Josef Schneider
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  3. Rudolf Geyer
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  4. Horst Ahorn
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  5. Ingrid Maurer-Fogy
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Kalsner, I., Schneider, FJ., Geyer, R. et al. Comparison of the carbohydrate moieties of recombinant soluble Fcε receptor (sFcε RII/sCD23) expressed inSaccharomyces cerevisiae and Chinese hamster ovary cells. Different O-glycosylation sites are used by yeast and mammalian cells. Glycoconjugate J 9, 209–216 (1992). https://doi.org/10.1007/BF00731167

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  • DOI: https://doi.org/10.1007/BF00731167

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