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Role of ß2-glycoprotein I in the anticardiolipin antibody affinity for phospholipid in autoimmune disease

Laboratory of Immunology, Brest University Medical School, BP 824, F29 609 Brest

J.C. Piette

Department of Internal Medicine, La Pitié-Salpétrière Hospital, Paris

M. Le Tonquèze

Laboratory of Immunology, Brest University Medical School, BP 824, F29 609 Brest

B. Bendaoud

Laboratory of Immunology, Brest University Medical School, BP 824, F29 609 Brest

R. Roué

Begin Hospital, Saint Mandé, France

M. Garré

Department of Internal Medicine, Brest University Medical School, BP 824, F29 609 Brest Cedex

P. Youinou

Laboratory of Immunology, Brest University Medical School, BP 824, F29 609 Brest

The binding capacity to cardiolipin and the functional affinity of affinity-purified anticardiolipin (aCL) IgG of patients with autoimmune disease have been compared with those of individuals with malaria and acquired immunodeficiency syndrome (AIDS). The binding of autoimmune IgG aCL was enhanced gradually by the incorporation of increasing amounts of ß₂-glycoprotein I (ß₂GPI) into the assay, in contrast to that of patients with infectious diseases. In addition, there were significant reductions of functional affinity in autoimmune disease, but not in malaria or in AIDS. These results indicate that ß₂GPI requirement for binding to the target antigen varies inversely with functional affinity in autoimmune disease when ß ₂GPI was present, and suggest that IgG aCL are more heterogeneous in this type of disorder than in patients with infectious disease.

Key Words: anticardiolipin antibody • ß2-glycoprotein I • functional affinity

Lupus, Vol. 4, No. 6, 477-481 (1995)
DOI: 10.1177/096120339500400610


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