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Review : Epitopes on β2-GPI recognized by anticardiolipin antibodies

Department of Medicine , Hokkaido University School of Medicine, Sapporo Japan

K. Ichikawa

Department of Medicine , Hokkaido University School of Medicine, Sapporo Japan

H. Kasahara

Department of Medicine , Hokkaido University School of Medicine, Sapporo Japan

T. Atsumi

Department of Medicine , Hokkaido University School of Medicine, Sapporo Japan

A. Tsutsumi

Department of Medicine , Hokkaido University School of Medicine, Sapporo Japan

E. Matsuura

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

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.

Key Words: anticardiolipin antibodies • β2-glycoprotein I • epitopes • structure of β2-GPI

Lupus, Vol. 7, No. 2 suppl, S14-S17 (1998)
DOI: 10.1177/096120339800700204


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