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 language | English |
---|---|
Pages (from-to) | S14-S17 |
Journal | Lupus |
Volume | 7 |
Issue number | SUPPL. 2 |
DOIs | |
Publication status | Published - 1998 |
Keywords
- Anticardiolipin antibodies
- Epitopes
- Structure of β-GPI
- β-glycoprotein I
ASJC Scopus subject areas
- Rheumatology