The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59

  • Pauline M. Rudd
  • B. Paul Morgan
  • Mark R. Wormald
  • David J. Harvey
  • Carmen W. van den Berg
  • Simon J. Davis
  • Michael A. J. Ferguson
  • Raymond A. Dwek
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 435)


CD59 is a cell surface glycoprotein that binds to the complement proteins C8 and/or C9 in the nascent membrane attack complex, thereby protecting host cells from lysis (1). CD59 belongs to the Ly-6 superfamily (2) and is present on a wide variety of cell types, including leukocytes, platelets, epithelial and endothelial cells, placental cells and erythrocytes, where it is present at 2.5–5 × l04 copies/cell (3). In addition to its role in protecting host tissues from homologous complement, it has been proposed that CD59 mediates T-cell adhesive interactions by synergising with CD58 via direct interactions with CD2 (4,5) although this is controversial (6,7). It has also been proposed that CD59 participates in T cell activation pathways and platelet secretory responses (1).


Normal Phase HPLC Elution Position Inositol Ring Exoglycosidase Digestion Biantennary Glycan 
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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Pauline M. Rudd
    • 1
  • B. Paul Morgan
    • 2
  • Mark R. Wormald
    • 1
  • David J. Harvey
    • 1
  • Carmen W. van den Berg
    • 2
  • Simon J. Davis
    • 4
  • Michael A. J. Ferguson
    • 3
  • Raymond A. Dwek
    • 1
  1. 1.Glycobiology Institute, Department of BiochemistryUniversity of OxfordOxfordUK
  2. 2.Department of Medical BiochemistryUniversity of Wales College of MedicineCardiffUK
  3. 3.Department of BiochemistryUniversity of DundeeDundeeScotland
  4. 4.Molecular Sciences Division, Nuffield Department of Clinical MedicineUniversity of Oxford, John Radcliffe HospitalHeadington, OxfordUK

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