Fig. 2: Receptor-binding properties of the wild-type H2N2 avian and human viruses. | Nature Communications

Fig. 2: Receptor-binding properties of the wild-type H2N2 avian and human viruses.

From: Dual receptor-binding, infectivity, and transmissibility of an emerging H2N2 low pathogenicity avian influenza virus

Fig. 2: Receptor-binding properties of the wild-type H2N2 avian and human viruses.

a–c Receptor-binding properties at the virus level. Results of the solid-phase binding assays for Dk/FJ/2021 (a), A/SG/1/1957 (b), and A/KR/426/1968 (c) to both α2,3-linked (3′-SLNLN) and α2,6-linked (6′-SLNLN) sialylglycan receptors. Blue and red lines represent 3′-SLNLN and 6′-SLNLN, respectively. Vaccine strains (A/SG/1/1957 and A/KR/426/1968) were rescued by reverse genetics, in which HA and NA genes from the wild-type A/SG/1/1957 or A/KR/426/1968 strains and the internal genes from the vaccine backbone A/PR/8/34. A/CA/04/2009 and A/VN/1194/2004 were used as controls. d–f Receptor-binding properties at the protein level. BIAcore diagram of HAs from Dk/FJ/2021 (d), A/SG/1/1957 (e), and A/KR/426/1968 (f) binding to 3′-SLNLN or 6′-SLNLN. The binding affinity (KD) values were calculated using the BIAcore 3000 analysis software (BIAcore version 4.1). The binding curve to the 3′-SLNLN is shown in blue, and that for the 6′-SLNLN is shown in red.

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