Alternative roles for CD59

Mol Immunol. 2007 Jan;44(1-3):73-81. doi: 10.1016/j.molimm.2006.06.019. Epub 2006 Aug 1.


CD59 was first identified as a regulator of the terminal pathway of complement, which acts by binding to the C8/C9 components of the assembling membrane attack complex (MAC), to inhibit formation of the lytic pore. Structurally, CD59 is a small, highly glycosylated, GPI-linked protein, with a wide expression profile. Functionally, the role of CD59 in complement regulation is well-defined but studies have also shown clear evidence for signalling properties, which are linked to its glycophosphatidyl inositol (GPI) anchor and its location within lipid rafts. Cross-linking of CD59 using specific monoclonal antibodies drives both calcium release and activation of lipid-raft associated signalling molecules such as tyrosine kinases. These observations clearly show that CD59 exhibits roles independent of its function as a complement inhibitor. In this review, we examine the progression of research in this area and explore the alternative functions of CD59 that have recently been defined.

Publication types

  • Review

MeSH terms

  • Animals
  • B-Lymphocytes / physiology
  • Bacterial Proteins / physiology
  • Bacteriocins
  • CD2 Antigens / physiology
  • CD59 Antigens / physiology*
  • Calreticulin / physiology
  • Humans
  • Killer Cells, Natural / physiology
  • Lipopolysaccharides / pharmacology
  • Signal Transduction
  • T-Lymphocytes / physiology


  • Bacterial Proteins
  • Bacteriocins
  • CD2 Antigens
  • CD59 Antigens
  • Calreticulin
  • Lipopolysaccharides
  • intermedilysin protein, Streptococcus intermedius