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

    42 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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