The Analysis of the Structure of Receptor Binding Site of Hemagglutin in Molecule of Influenza A Virus and of the Characteristics of Receptor.

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We have studied the receptor binding structure on the hemagglutinin (HA) protein of the influenza A virus using two different methods.First, we synthesized cDNAs of the HA genes of influenza A virus which belong to seven different subtypes and whose nucleotide sequences were not reported until 1989. We compared the amino acid sequences which are composing the putative receptor binding structure among 13 serotype HA proteins and discussed the structural feature of the receptor binding site (ref 10).Secondly, we constructed several mutant HA cDNAs by site-directed mutagenesis and expressed them in mamalian cells. We found that the amino acid residue 226 on the HA protein of the H1 subtype was important for the receptor binding (ref 3, 10).We also investigated the amino acid changes on the HA proteins of the H1 and H3 subtypes of human influenza A virus during the evolution of each subtype and discussed the influence of these amino acid changes to the receptor binding site (ref 2, 4, 9).We have investigated the receptor specificity of HA proteins among 13 different subtypes. We found all HA proteins except H3 subtype have glutamin at the amino acid residue 226, but they bind to Neu2-6Gal or Neu2-3 Gal (ref. 10)