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  • Title: Structural requirements for addition of O-linked carbohydrate to recombinant erythropoietin.
    Author: Elliott S, Bartley T, Delorme E, Derby P, Hunt R, Lorenzini T, Parker V, Rohde MF, Stoney K.
    Journal: Biochemistry; 1994 Sep 20; 33(37):11237-45. PubMed ID: 7727375.
    Abstract:
    To define the structural requirements for addition of O-linked glycosylation in vivo, recombinant erythropoietin (rEPO) variants were constructed. Thirty-three independent Ser or Thr substitutions were constructed and examined to see which were subject to O-linked carbohydrate addition. Variants with Thr mutations at positions 123 and 125, but not elsewhere, contained additional carbohydrate, which suggests that several positions around the existing O-linked glycosylation site (Ser126), but not elsewhere, contain the necessary information for O-linked carbohydrate addition. Two forms of the Thr125 variant were identified. One form was glycosylated only at residue 125, and a second form was glycosylated at both Thr125 and Ser126, the normal O-glycosylation site. We have also found that glycosylation is less efficient when rEPO is improperly folded and that prolines at -1 and +1 relative to the O-glycosylation site enhance glycosylation.
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