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. 2024 Oct 10;98(11):e01052-24. doi: 10.1128/jvi.01052-24

Fig 1.

Two diagrams showing amino acid sequence alignment for various H5N1 and H5N8 influenza strains and glycan-binding profiles for different neuraminic acid species and linkages. Bar graph shows HA binding strength, as measured by hemagglutination titers

(A) HA receptor binding site amino acid alignment of the H5 hemagglutinins used in this study. Alignment of the receptor binding site residues with amino acid positions (H3 numbering) indicated above the alignment, non-conserved residues are highlighted in black, and dots indicate identical amino acids. Several mammalian sequence isolates in North America are shown to demonstrate the close relationship. (B) Overview of lectin specificity to differentially linked unmodified and modified SIA. Black boxes indicate core specificities, and gray boxes indicate possible ligands. (C) Hemagglutination assay with chicken erythrocytes with the lectins used for tissue stain.