Human influenza virus recognition of sialyloligosaccharides

Abstract
Sialic acids are essential components of cell‐surface receptors utilized by influenza viruses. To evaluate the recognition of asialic sugar parts of the receptor, three representative strains of human influenza A and B viruses were tested for their binding of a panel of sialyloligosaccharides. The highest affinity binding carbohydrate determinants recognized by the viruses in a context of different core structures were Neu5Acα2‐3Gal for the type B virus, Neu5Acα2‐6Gal for the H3 subtype virus, and Neu5Acα2‐6Ga/β1‐4GlcNAc for the H1 subtype virus. Penultimate to these determinants parts of sialyloligosaccharides studied either contributed less significantly to the binding affinity, or interfered with the binding.