Koike T, Ichikawa K, Kasahara H, Atsumi T, Tsutsumi A, Matsuura E
Department of Medicine II, Hokkaido University School of Medicine, Sapporo, Japan.
Lupus. 1998;7 Suppl 2:S14-7. doi: 10.1177/096120339800700204.
Anticardiolipin antibodies (aCL) found in sera from patients with antiphospholipid syndrome recognize a cryptic epitope that appears on the beta2-glycoprotein I (beta2-GPI) molecule when beta2-GPI interacts with a lipid membrane composed of negatively charged phospholipid or when beta2-GPI is adsorbed on a polyoxygenated polystyrene plate. A homology based model of beta2-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 beta2-GPI.
抗磷脂综合征患者血清中发现的抗心磷脂抗体（aCL）识别一种隐蔽表位，当β2-糖蛋白I（β2-GPI）与由带负电荷磷脂组成的脂质膜相互作用时，或当β2-GPI吸附在多氧化聚苯乙烯板上时，该表位出现在β2-GPI分子上。基于人因子H的寿司结构域的核磁共振坐标构建了β2-GPI的同源模型。其构象像一个由五个结构域组成的圆柱体，其四结构域和五结构域通过静电相互作用结合在一起。我们使用噬菌体展示随机肽库来搜索人aCL的表位。在β2-GPI的四结构域上发现了与通过生物淘选方法选择的共有序列相似的结构。
