Fig. 2: 42D6 is a potent strain-transcending neutralizing Ab targeting a distinct epitope that partially overlaps with sites bound by non-neutralizing Abs. | Nature Communications

Fig. 2: 42D6 is a potent strain-transcending neutralizing Ab targeting a distinct epitope that partially overlaps with sites bound by non-neutralizing Abs.

From: Neutralizing and interfering human antibodies define the structural and mechanistic basis for antigenic diversion

Fig. 2

a Epitope binning for the p19-specific human mAbs. Primary saturating antibodies tested are listed in the left column, while secondary competing antibodies are listed at the top in rows. Data indicate the percent of competing antibody binding compared to the maximum competing antibody response in the absence of the primary antibody. Boxes are colored according to competition status. Antibodies that displayed ≤50% maximal binding are colored light red and are considered “competing”. Negative values were normalized to 0. b Crystal structures of p19 bound to the Fab fragment of 42D6 (bright orange), 42C11 (light blue), and 42C3 (light green). All crystal structures are shown according to the same p19 orientation. p19 is represented as white surface. c Structural basis for the inhibition of parasite growth by p19-specific hmAb 42D6. Superposition of p19-Fab co-complex crystal structures. p19 is represented as white surface and Fabs are shown as cartoon representation and colored as in b. The epitope for non-neutralizing hmAb MaliM03 (PDB ID: 6XQW) and murine mAb G17.12 (PDB ID: 1OB1) is colored in magenta and Fab fragment of MaliM03 and G17.12 are colored in light magenta and light pink, respectively. The potent neutralizing hmAb 42D6 is shown to recognize a novel epitope on p19.

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