Fig. 4: HA-K130N and HA-K130E mutations affect receptor binding affinity. | Nature Communications

Fig. 4: HA-K130N and HA-K130E mutations affect receptor binding affinity.

From: A primary oseltamivir-resistant mutation in influenza hemagglutinin and its implications for antiviral resistance surveillance

Fig. 4: HA-K130N and HA-K130E mutations affect receptor binding affinity.

a Crystal structure of influenza A/California/04/2009 (Cal09) virus hemagglutinin (HA) complexed with human receptor analog (PDB ID: 4JTV). b–d Ribbon representation of structural models of HA-WT (b), HA-K130N (c), and HA-K130E (d) in complex with the human receptor. The residues 130 and 142 of HA are shown. Potential interactions between the protein and the receptors are represented by broken lines. e–g Surface representation of structural models of HA-WT (e), HA-K130N (f), and HA-K130E (g) in complex with the human receptor, colored by electrostatic potential (red negative, blue positive). The locations of the HA 130 residue are indicated by a dotted circle. h, i BIAcore plots showing binding of Cal09 HA-WT, HA-K130N, and HA-K130E to α-2,6-linked sialylglycan human (h) and α-2,3-linked sialylglycan avian (i) receptors. The HA protein of avian H5 subtype virus acts as a positive control for specific binding to α-2,3-linked sialylglycan avian receptor. 200 μM of Cal09-WT or mutant proteins and 10 μM of H5 protein, were used for kinetics analysis. Source data are provided as a Source Data file.

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