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One has to take into account that when the antibody is binding to common epitopes, this antibody is going to be cross-reactive with related proteins sharing these epitopes when also present in the mix.
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These results indicate that PNP autoantibodies bind to common epitopes present on both p170 and A2ML1.
The layer formation seems to hinder aPL binding to β2GPI epitopes close to D5 [16].
Both the mouse 13H11 MAb and the three prototypic cluster II human MAbs (98-6, 126-6, and 167-D) blocked 2F5 binding to gp41 epitopes to variable degrees; the combination of 98-6 and 13H11 completely blocked 2F5 binding.
Epitope mapping was performed with all antibodies to verify binding to linear epitopes.
ICR65, however, cross-reacted with mAbs binding to both epitopes.
Ligands binding to distinct epitopes on the same target molecule may influence each other, for example, inhibiting binding to adjacent epitopes.
The competitive inhibition of binding to overlapping epitopes has been described for antibodies to ACE.
Ligands binding to distinct epitopes of anchoring molecules may enter cells differently.
The development of an antibody response involves different cells of the immune system, but the final common pathway involves expansion and differentiation of B-cells with antibody receptors capable of binding to epitopes on the protein therapeutic.
The inhibition is mediated via antibody binding to epitopes outside of the CD81 binding site in E2, possibly by preventing conformational changes in E2 that are required for CD81 binding.
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