Figure 5: E190D in the HA RBS favors binding against VPGSGW. | Nature Communications

Figure 5: E190D in the HA RBS favors binding against VPGSGW.

From: In vitro evolution of an influenza broadly neutralizing antibody is modulated by hemagglutinin receptor specificity

Figure 5

The hydrogen bond network involving S100d of the CDR H3 of VPGSGW is shown for (a) binding against HA RBS of HK68/H3, and (b) binding against HA RBS of HK68/H3 that carried mutation E190D, which is modelled based on the crystal structure of VPGSGW-HK68/H3 HA1. A putative sodium ion is represented by the purple sphere. For visual clarity, only G100c, S100d, G100e, and W100f on the Fab are displayed. (c) The affinities of WT C05 Fab (VVSAGW) and a C05 Fab variant (VPGSGW) against the HA from A/Hong Kong/1/1968 (wild type: E190; E190D mutant: D190) are shown as a bar chart. (d,e) The neutralizing activity of WT C05 and VPGSGW in IgG format against (d) SI06-HA/WSN virus, and (e) A/Aichi/2/68 virus were measured by cell viability assay. SI06-HA/WSN virus was generated based on WSN, in which the HA ectodomain was replaced by that from SI06 (see Methods). Colour code is the same as that of c. Mean value across three replicates is shown and the error bar represents the s.d. The large error bar in VPGSGW at 100 μg ml−1 against A/Aichi/2/68 virus is due to complete protection in one but not in the other two replicates.

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