Adjustment of receptor-binding and neuraminidase substrate specificities in avian-human reassortant influenza viruses.

Balanced action of hemagglutinin (HA) and neuraminidase (NA) is an important condition of influenza virus efficient replication, but a role of HA and NA specificities at oligosaccharide level in maintaining such a balance remains poorly studied. Avian virus HA binds exclusively and NA digests efficiently alpha2-3-sialylated carbohydrate chains, while human virus HA interacts with alpha2-6 chains and low-active NA cleaves both alpha2-3- and alpha2-6-sialosides. Reassortment between viruses leading to appearance of avian virus HA and human virus NA on the virion surface often resulted in decreasing the replicative potential of the formed variants because of disturbance of a functional balance between "alien" HA and NA.