Impact of a potential glycosylation site at neuraminidase amino acid 264 of influenza A/H9N2 virus

Abstract

To determine the role of the potential glycosylation site NA264N, which has been shown to be prevalent in recent Chinese H9N2 isolates, four reverse genetic viruses, rgWS1-NA264N, rgWS1-NA264H, rgBJ-NA264H and rgBJ-NA264N, were rescued. Growth kinetics showed that viruses with NA264H grew faster than viruses with NA264N. Mouse studies revealed that rgBJ-NA264H replicated to a significantly higher titer than rgBJ-NA264N at 3dpi. Notably, in contact chickens, rgBJ-NA264H and rgWS1-NA264H shed significantly more virus than rgBJ-NA264N at 6dpi from the larynx and rgWS1-NA264N at 4dpi from the cloaca, respectively. The present study demonstrates that NA264N affects viral replication of H9N2.

Keywords: H9N2; NA264N; Pathogenesis; Viral replication; Virus rescuing.