Epitope fine specificity of human anti-HLA-A2 antibodies. Identification of four epitopes including a haptenlike epitope on HLA-A2 at lysine 127.
Anti-HLA-A2 CREG antibodies were purified from seven individuals by affinity chromatography. The binding of the purified antibodies to single or multiple amino acid variants of HLA-A2.1 was measured with an inhibition RIA. Substitutions at 10 amino acid residues in the polymorphic alpha 1 and alpha 2 domains were important for human antibody binding; eight of these have previously been shown to be important in the binding of murine anti-HLA-A2 CREG antibodies. Unlike any previously reported murine mAbs, the binding of antibodies from two individuals was eliminated by a substitution at the HLA-A2, -24, -28 shared loop amino acid residue lysine 127. Conversely, when the asparagine at residue 127 on the non-cross-reactive HLA-A3 was replaced with lysine, antibody binding was completely restored. The results further suggest that both lambda- and kappa-containing human antibodies that bind to this region may recognize lysine 127 as a haptenlike epitope. Anti-HLA-A2 antibodies that recognized a conformational epitope defined by changes at glycine 62 in the alpha 1 domain were predominated by lambda light chains whereas those that recognize an epitope defined by a loop residue at tryptophan 107 in the alpha 2 domain were predominated by kappa light chains. The data are consistent with a model of restricted epitope recognition of HLA-A2 by human B cells that is similar to, but distinct from, epitope recognition by mouse B-cell hybridomas, and may help to explain the phenomenon of public or cross-reactive idiotypes in the HLA system.[1]References
- Epitope fine specificity of human anti-HLA-A2 antibodies. Identification of four epitopes including a haptenlike epitope on HLA-A2 at lysine 127. De Vito, L.D., Mason, B.P., Jankowska-Gan, E., Hogan, K.T., Guo, J.W., Lutz, C.T., Sollinger, H.W., Burlingham, W.J. Hum. Immunol. (1993) [Pubmed]
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