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[Preprint]. 2024 Jul 31:2024.07.30.605893. [Version 1] doi: 10.1101/2024.07.30.605893

Fig. 1. Receptor binding specificity of bovine H5N1.

Fig. 1.

(a) Structures of glycans printed on the microarray. All N-glycans (A-X) have an α-amine at the reducing end asparagine moiety and O-glycans (1-5) have a N-terminal α-amine. (b) Glycan array binding analysis of the receptor binding specificities of H5N1 and H1N1 viruses. The fluorescence signals for each glycan are presented as mean ± SD (n = 4). (c) Bio-layer interferometry (BLI) sensorgrams demonstrating the sialic acid linkage-specificity of H5N1 and H1N1 viruses. Virus binding (association, in the presence of Oseltamivir,) and virus elution (dissociation, in the absence of Oseltamivir, gray highlighted) are shown. Representative data of at least two replicate experiments are shown.