Epitopes on β2-GPI recognized by anticardiolipin antibodies

T. Koike, K. Ichikawa, H. Kasahara, T. Atsumi, A. Tsutsumi, E. Matsuura

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)


Anticardiolipin antibodies (aCL) found in sera from patients with antiphospholipid syndrome recognize a cryptic epitope that appears on the β2-glycoprotein I (β2-GPI) molecule when β2-GPI interacts with a lipid membrane composed of negatively charged phospholipid or when β2-GPI is adsorbed on a polyoxygenated polystyrene plate. A homology based model of β2-GPI was constructed based on the NMR coordinates of sushi domains of human factor H. The conformation was like a cylinder consisting of five domains, its IV and V domains being glued by electrostatic interaction. We used phage-displayed random peptide libraries to search the epitopes of human aCL. Structures similar to consensus sequences selected by a biopanning method was found on domain IV of β2-GPI.

Original languageEnglish
Pages (from-to)S14-S17
Issue numberSUPPL. 2
Publication statusPublished - 1998


  • Anticardiolipin antibodies
  • Epitopes
  • Structure of β-GPI
  • β-glycoprotein I

ASJC Scopus subject areas

  • Rheumatology


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