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International Immunology Advance Access originally published online on October 12, 2005
International Immunology 2005 17(12):1533-1542; doi:10.1093/intimm/dxh330
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© The Japanese Society for Immunology. 2005. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Antigenic structures recognized by anti-ß2-glycoprotein I auto-antibodies

Hideki Kasahara1, Eiji Matsuura2, Keiko Kaihara2, Daisuke Yamamoto3, Kazuko Kobayashi2, Junko Inagaki2, Kenji Ichikawa1, Akito Tsutsumi1, Shinsuke Yasuda1, Tatsuya Atsumi1, Tatsuji Yasuda2 and Takao Koike1

1 Department of Medicine II, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan
2 Department of Cell Chemistry, Okayama University Graduate School of Medicine and Dentistry, Okayama 700-8558, Japan
3 Biomedical Computation Center, Osaka Medical College, Takatsuki 569-8686, Japan

Correspondence to: T. Koike; E-mail: tkoike{at}med.hokudai.ac.jp

ß2-Glycoprotein I (ß2-GPI) is a major antigen for anti-cardiolipin antibodies and their epitopes are cryptic. Conformation of each domain of ß2-GPI was optimized from its crystal structure by energy minimization and by molecular dynamics simulation. Three electrostatic interactions, i.e. D193–K246, D222–K317 and E228–K308, were observed between domains IV and V in the optimized structure that was constructed based on the consensus sequences obtained by the phage-displayed random peptide library. Antigenic structures determined by the epitope mapping mainly consisted of hydrophobic amino acids located on two discontinuous sequences in domain IV. These amino acid clusters, as an epitope, were covered by domain V and were of a hidden nature. A similar but incomplete counterpart to the epitopic clusters was found in domain I but was not in domains II or III. Binding of anti-ß2-GPI auto-antibodies to solid-phase ß2-GPI was significantly reduced either by L replacement for W235, a common amino acid component for the epitopes, or by V replacement for all of D193, D222 and E228. Structural analysis indicated a hypothesis that these electrostatic interactions between domains IV and V retained exposure to W235 and that epitope spreading occurred in the region surrounding W235. Thus, epitopic structures recognized by anti-ß2-GPI auto-antibodies are cryptic and inter-domain electrostatic interactions are involved in their in exposure.

Keywords: anti-phospholipid antibody, anti-phospholipid syndrome, B cell epitope

Transmitting editor: S. Izui


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