Epitopes on β2-GPI recognized by anticardiolipin antibodies

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

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41 Citations (Scopus)

Abstract

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
JournalLupus
Volume7
Issue numberSUPPL. 2
DOIs
Publication statusPublished - 1998

Keywords

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

ASJC Scopus subject areas

  • Rheumatology

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    Koike, T., Ichikawa, K., Kasahara, H., Atsumi, T., Tsutsumi, A., & Matsuura, E. (1998). Epitopes on β2-GPI recognized by anticardiolipin antibodies. Lupus, 7(SUPPL. 2), S14-S17. https://doi.org/10.1177/096120339800700204