Heterogeneity of antibodies to 2-glycoprotein 1 from patients with systemic lupus erythematosus

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Abstract
We studied antibodies to β2-glycoprotein 1 (anti-β2 GP1) from 72 patients with systemic lupus erythematosus (SLE) with or without antiphospholipid syndrome (APS) or with or without anticardiolipin antibodies (aCL). Fifteen patients had APS and positive antiphospholipid antibodies [clinical APS()/aPL()], 12 patients had APS, negative serum IgG and IgM aCL, anti-phosphatidylethanolamine, anti-phosphatidylserine and no lupus anticoagulant [clinical APS()/aPL(-)]. A third group included 16 patients without APS but high aCL levels [clinical APS(-)/aPL()]. In a fourth group we studied 29 patients without clinical manifestations of APS or aCL [clinical APS(-)/aPL(-)]. One hundred anticardiolipin and VDRL-negative normal sera were studied as controls. IgG antibodies to cardiolipin proper in a bovine β2 GP-free system, to human b2GP1 immobilized on cardiolipinor to human β2 GP1 alone were detected in all sera by ELISA using irradiated and nonirradiated plates from two manufacturers. Sera from APS()/aPL() patients showed IgG binding to CL, CL β2 GP1 and β2 GP1 in irradiated and nonirradiatedplates. APS()/aPL(-) sera had more significant IgG binding to β2 GP1 than normal controls when studied in both irradiated or nonirradiatedplates (P 0.001). This binding was inhibited by solid-phase cardiolipin in a dose-dependentmanner. Sera from the APS(-)/aPL() subgroup had comparable IgG activity in both the CL and CL β2 GP1 assays, while no anti-β2 GP1 activity was detected in these sera. Sera from the clinical APS(-)/aPL(-) patients were negative in the three ELISA systems. Antibodies to human β2 GP1 from SLE patients recognize various epitopes. Those from APS()/aPL() patients appear to react with an epitope boosted by cardiolipin in addition to another one present in the native protein. In contrast, anti-β2 GP1 from patients with APS()/aPL(-) are blocked by cardiolipin, suggestingthat their epitope is the phospholipid-binding site.
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