Anticardiolipin and anti-beta(2)-GPI are two distinct populations of autoantibodies

This study has been undertaken to assess whether anticardiolipin and anti-beta(2)-GPI are two distinct populations of (auto)antibodies, and to clarify whether the beta(2)-GPI region critical for phospholipid binding is also crucial for anti-beta(2)-GPI reactivity. Fourteen of the 62 anticardiolipin (aCL) ELISA positive sera (22.6%) were positive for anti-beta(2)-GPI by immunoblotting, 42 (67.7%) for aCL using TLC immunostaining. IgG fractions from 5 sera gave the same anticardiolipin reactivity detected by TLC immunostaining in the corresponding sera. All anti-beta(2)-GPI-positive sera were reactive with the phenylthio-carbamyl derivative of the protein, indicating that binding of phenylisothiocyanate with lysine residues does not modify the molecule antigenicity. In addition, incubation of IgG fractions with the phospholipid binding site did not modify reactivity with beta(2)-GPI. These findings demonstrate that: a) ''true'' antiphospholipid antibodies are detectable in patients' sera; b) aCL and anti-beta(2)-GPI have a different immunological profile; c) the beta(2)-GPI phospholipid-binding site is not the region recognized by the antibodies.