Fig. 7: Glycan binding by additional HA variants. | Nature Communications

Fig. 7: Glycan binding by additional HA variants.

From: Probing altered receptor specificities of antigenically drifting human H3N2 viruses by chemoenzymatic synthesis, NMR, and modeling

Fig. 7

a, b Glycan binding by NL09 HA. MD derived complex structure with 2 (a), and 1H[13C]-STD intensities from the 2D 1H-STD-1H,13C-HSQC spectrum of 3–5 (b). c Comparison of 1H[13C]-STD signals of 5 in the presence of Sing16 HA and its Y159A HA mutant. The STD spectra are offset, in the vertical 13C dimension, to allow a comparison of their intensities. Note the significantly weaker STD signals for mutant Sing16 Y159A HA relative to the wild type. d 1H-STD intensities for the 13C-labeled galactoside residue in 5. e, f Model of glycan-HA interactions in Sing16 HA (e) and its Y159A HA mutant (f). The absence of an aromatic moiety in the Y159A mutant precludes the key CH-π interaction with Gal-6.

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