Epitopes on β2-GPI recognized by anticardiolipin antibodies

Author:

Koike T1,Ichikawa K1,Kasahara H1,Atsumi T1,Tsutsumi A1,Matsuura E2

Affiliation:

1. Department of Medicine II, Hokkaido University School of Medicine, Sapporo Japan

2. Department of Cell Chemistry, Institute of Molecular and Cellular Biology, Okayama University Medical School, Okayama, Japan

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.

Publisher

SAGE Publications

Subject

Rheumatology

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