HA receptor-binding specificity is a major molecular determinant for the host range of influenza viruses. Amino acids at positions 226 and 228 of HA are critical for specificity of receptor-binding in influenza viruses. Within the HA protein of novel H7N9 viruses, there was a leucine residue at position 226, which is characteristic of the HA gene in human influenza viruses. This finding implies that H7N9 viruses have partially acquired human receptor-binding specificity. All of the H7N9 human isolates examined contained a lysine residue at position 627 in the PB2 protein. It is well known that this lysine residue contributes to the replication and transmission of avian influenza viruses in mammalian hosts. It is likely that the acquisition of this lysine in H7N9 viruses during their replication in human hosts has significantly contributed to their virulence and lethality in humans.
Tracing the source of these novel H7N9 influenza viruses, and their subsequent characterization, was a collaborative effort involving researchers from the National Avian Influenza Reference Laboratory at the Harbin Veterinary Research Institute, and Shanghai Animal Disease Control Center. This research project was partially supported by the National Basic Research Program of China (2011CB505000), the China Agriculture Research System (CARS-42-G08), and the National Science and Technology Major Project (2012ZX10004214). We suggest that strong measures, such as continued surveillance of avian and
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