Fig. 2: Structural analysis of the 22C10 Fab fragment in complex with PDCoV S trimer. | Nature Communications

Fig. 2: Structural analysis of the 22C10 Fab fragment in complex with PDCoV S trimer.

From: Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein

Fig. 2

A Surface representation of the trimeric PDCoV S bound to three 22C10 antibody Fab fragments. S protein protomers are in blue, gray, and pink, respectively. The Fab variable light chain is colored in purple and variable heavy chain labeled in yellow. B Atomic model of a single PDCoV S1A domain in complex with the 22C10 Fab fragment, including the interaction site of PDCoV S 22C10 Fab fragment. S1A is colored in blue and viral escape mutations highlighted in red. Fab variable light is colored in medium purple and variable heavy labeled in yellow. C PDCoV S protomer comparison, left-PDCoV S protomer only and right-22C10 Fab fragment bound PDCoV S. The N-terminus, unresolved in the apo structure, is highlighted in red, and major architectural changes are marked with arrows. D Mapping of PDCoV amino acid conservation onto the surface representation of PDCoV S1A domain, with the 22C10 Fab fragment bound. E ELISA binding reactivity of 22C10 to PDCoV S1 variants carrying the indicated mutations. Results represent the mean (±SD) from two independent experiments with two or three technical replicates. Source data are provided as a Source Data file.

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