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• W2149292764 abstract "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." @default.
• W2149292764 created "2016-06-24" @default.
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• W2149292764 date "2003-12-01" @default.
• W2149292764 modified "2023-09-26" @default.
• W2149292764 title "Anti-cardiolipin/β-2 glycoprotein activities co-exist on human anti-DNA antibody light chains" @default.
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• W2149292764 doi "https://doi.org/10.1016/s0161-5890(03)00225-6" @default.
• W2149292764 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14563371" @default.
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