Open Accessβ 2 ‐Glycoprotein i reactivity of monoclonal anticardiolipin antibodies from patients with the antiphospholipid syndrome
Author(s) -
Ichikawa Kenji,
Khamashta Munther A.,
Koike Takao,
Matsuura Eiji,
Hughes Graham R. V.
Publication year - 1994
Publication title -
arthritis & rheumatism
Language(s) - English
Resource type - Journals
eISSN - 1529-0131
pISSN - 0004-3591
DOI - 10.1002/art.1780371008
Subject(s) - monoclonal antibody , epitope , monoclonal , microbiology and biotechnology , glycoprotein , antiphospholipid syndrome , epitope mapping , chemistry , antibody , immunology , medicine , biology
Objective . To elucidate the specificity of anticardiolipin antibodies (aCL) from patients with the antiphospholipid syndrome (APS) to various phospholipids (PLs), DNA, and β 2 ‐glycoprotein I (β 2 ‐GPI). Methods . Five monoclonal aCL were established from peripheral blood lymphocytes of 3 patients with the APS. The reactivity of monoclonal aCL with various PLs, with DNA, and with β 2 ‐GPI was examined by enzyme‐linked immunosorbent assay (ELISA). Results . All of the monoclonal aCL bound to anionic PLs, only in the presence of β 2 ‐GPI. Neither monoclonal aCL nor β 2 ‐GPI bound to DNA. Monoclonal aCL bound to solid‐phase β 2 ‐GPI on polystyrene ELISA plates that had carboxyl groups on their surface, but did not react with solid‐phase β 2 ‐GPI on ordinary polystyrene plates. A mixture of β 2 ‐GPI and CL inhibited the binding of monoclonal aCL to β 2 ‐GPI, but CL or β 2 ‐GPI alone did not. Conclusion . Monoclonal aCL may recognize a cryptic epitope, which appears as a result of β 2 ‐GPI binding to anionic PLs or to polystyrene with carboxyl groups.