Abstract
Recent human H3N2 influenza viruses isolated in Japan and China were characterised from an evolutionary point of view. They appeared to have divided into three minor branch clusters, including 1992-1993, 1993-1994 and 1994-1995 isolates. It was of particular interest to reveal that in addition to amino acid substitutions in the antigenic sites of the HA molecule, amino acid changes occurred at position 226 of the receptor binding site from lysine or glutamine to isoleucine in all strains belonging to the 1994-1995 branch cluster. This is the first evidence of human H3N2 influenza isolates, or any other influenza HA serotypes, to contain a conserved amino acid residue other than lysine or glutamine at this key position.
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