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Publication Detail
Anti-cardiolipin/beta-2 glycoportein activities co-exist on human anti-DNA antibody light chains
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Kumar S, Nagl S, Kalsi JK, Ravirajan CT, Athwal D, Latchman DS, Pearl LH, Isenberg DA
  • Publication date:
  • Pagination:
    517, 530
  • Journal:
    Molecular Immunology
  • Volume:
  • Print ISSN:
  • Keywords:
    activity, anti-DNA, antibodies, Antibody, CHAIN, chains, glycoprotein, LIGHT, Amino Acid Sequence, Anti-cardiolipin, Antibodies, Anticardiolipin, Antinuclear, Autoantibodies, beta, cardiolipin, chemistry, Cross Reactions, domain, experiments, genetics, Glycoproteins, hybrid, IM, IMMUNOGLOBULIN, IMMUNOGLOBULINS, Immunoglobulins, Fab, Light-Chain, immunology, interaction, LA, model, MODELS, Molecular Sequence Data, Protein Structure, Tertiary, REACTIVITY, Result, Structure, Support, Non-U.S.Gov't, Three-dimensional, Anti-cardiolipin, beta-2 glycoportein, antibody
We have recently shown that the human anti-DNA antibodies B3 and 33H11 also bind cardiolipin and that the anti-autoantigen activity resides predominantly on their lambda light chains. We now show that the two auto-antibodies possess strong reactivity to the plasma-protein 2-Glycoprotein I (beta2-GPI) also. Utilizing chain shuffling experiments involving an unrelated anti-p185 antibody 4D5 with insignificant reactivity to cardiolipin or to beta2-GPI, we now demonstrate that hybrid Fabs with constituent light chain, but not the heavy chain, of B3 or 33H11, exhibit anti-cardiolipin activity. Furthermore, the constructs possessing the auto-antibody-derived light chain also exhibited significant reactivity to beta2-GPI. The results suggest that anti-DNA, anti-cardiolipin and anti-beta2-GPI activities co-exist on the light chains of the antibodies studied and, importantly, these activities could be transferred to antibody constructs by their light chains alone. Computer-generated models of the three-dimensional structures of the auto-antibodies and their hybrids, suggest predominant interaction of their light chains with domain IV of beta2-GPI
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