Fig. 7: Competitive binding of 1F4 and 3H7 to overlapping epitopes on CVA6.
From: Molecular mechanisms of receptor recognition and antibody neutralization of coxsackievirus A6
a Superimposed cryo-EM density maps of CVA6-1F4 and CVA6-3H7 complexes. The maps are colored by radial distance. 1F4 Fab is shown in magenta. 3H7 Fab is shown in blue. b Footprint analysis of 1F4 and 3H7 on CVA6 surface. Contour lines mark KRM1 in orange, 1F4 Fab in yellow, and 3H7 Fab in white. c Surface representation of CVA6 protomer showing epitopes of 1F4 (light sea green) and 3H7 (orange red). Overlapping regions recognized by both antibodies are highlighted in magenta. d Summary of the epitopes and buried surface areas of the 1F4 and 3H7 MAbs. e Schematic of antibody competition assay by BLI. (Left) No competition: the second CVA6 MAb binds freely to immobilized virions, producing strong signal. (Right) Competition: the first antibody binds to overlapping epitope, blocking the second MAb binding and reducing signal. f, g BLI-based antibody competition assay. Immobilized CVA6-HeB virions were pre-incubated with buffer (reference) or the first antibody, then exposed to the second MAb 1F4 (f) or 3H7 (g). An anti-SARS-CoV-2 MAb served as control (gray curve). Sensorgrams show real-time binding signals of the second MAbs 1F4 (f) and 3H7 (g). Source data are provided as a Source Data file.
