Fig. 4: Structure basis of the interaction between H2N2 HAs and avian and human receptor analogs. | Nature Communications

Fig. 4: Structure basis of the interaction between H2N2 HAs and avian and human receptor analogs.

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

Fig. 4: Structure basis of the interaction between H2N2 HAs and avian and human receptor analogs.The alt text for this image may have been generated using AI.

The secondary structural elements of the RBS (130-loop, 140-loop, 190-helix, and 220-loop; H3 number) are labeled in the ribbon representation, together with selected residues in the stick representation. Hydrogen bonds are indicated by the dashed lines. a, b Molecular interactions of Dk/FJ/2021 wild-type HA with human (a) and avian (b) receptor analogs. c Comparison of the RBSs between the Dk/FJ/2021 HA-avian receptor complex (light pink) and the Dk/FJ/2021-S144N HA mutant-avian receptor complex (orange). A similar trans conformation for glycan binding showed no observable drift between the two complexes. d, e Molecular interactions of A/SG/1/1957 HA with human (d) and avian (e) receptor analogs. f Comparison of the RBSs between the A/SG/1/1957 HA-human receptor complex (cyan) and A/SG/1/1957-R137M HA mutant-human receptor complex (lavender). The human receptor analog shifts towards the 130-loop by 0.8 Å in the A/SG/1/1957-R137M complex. g Comparison of the RBSs between the A/SG/1/1957 HA-human receptor complex (cyan) and A/SG/1/1957-N144E HA mutant-human receptor complex (green). The human receptor analog shifts towards the 220-loop by 1.3 Å in the A/SG/1/1957-N144E complex. h Comparison of the RBSs between the A/SG/1/1957 HA-human receptor complex (cyan) and A/KR/426/1968 HA-human receptor complex (pale green). The human receptor analog shifts towards the 130-loop by 0.8 Å in the A/KR/426/1968 complex.

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