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. 2015 Jun 30;10(6):e0130811. doi: 10.1371/journal.pone.0130811

Fig 1. HD5 mAb is specific to B272, binds to recombinant B272, and blocks interaction with immunoregulatory cell receptors.

Fig 1

(A) ELISA results showed the specificity of HD5 and HD6 to B272 homodimers when challenged for different recombinant HLA class I complexes (-A1,-B7,-B13,-C7,-B27, and-B272). Control HC10 and W6/32 antibodies were used as positive and negative control, respectively. (B) Direct ELISA against HLA-G and B272 homodimers using HD5, HD6, HC10 and W6/32 antibodies showed specificity of HD5 and HD6 to immobilized B272 homodimers but not to HLA-G homodimers. (C-E) Recombinant B272, B27-free-heavy chain and HLA-B27 heterotrimers were immobilized into chips for kinetic characterization by SPR. C) HD5 and ligand (B272) have a Kd of 0.32 nM. Immobilized free-heavy chains (D) or HLA–B27 heterotrimers (E) did not interact with HD5 and Kd values were not fitted. (F) Blocking competition experiments in SPR were performed by immobilizing B272 to a streptavidin chip followed by injection of HD5 to form B272-HD5 complexes. Injections of LILRB2, KIR3DL2 and Pirb were assessed and binding events recorded.