Fig. 1From: Structural properties of immune complexes formed by viral antigens and specific antibodies shape the inflammatory response of macrophagesCharacterization of mAbs according to their epitopes. Competition of each mAb to bind the same epitope was evaluated by competitive ELISA. Firstly, unconjugated mAbs were added followed by mAb-HRP addition. OD values represent binding efficacy of mAb-HRP in the presence of unconjugated mAbs. OD of each mAb-HRP control was set as maximum value (100%) to evaluate the competition effect of unconjugated mAbs. The OD of each mAb (represented in A) was divided by this maximum value and expressed as the percentage of mAb-HRP binding (% of mAb-HRP in B). 100% indicates no competition, 50% – moderate competition and 0% – full competition/no binding. (C) Schematic representation of mAb (mAb-HRP) binding to VLPs in the presence of another mAb (unconjugated mAb). The absence of mAb-HRP (red) indicates that the epitope is fully occupied by another mAb (black, unconjugated mAb), one mAb-HRP indicates that mAb-HRP binds to adjacent epitope of unconjugated mAb epitope, and two mAb-HRP indicates that mAb-HRP binds to epitopes different from those of the unconjugated mAbs. C was created with BioRender.com, AG No.: ES268ORVA0Back to article page