Identification of amino acid residues of influenza A virus H3 HA contributing to the recognition of molecular species of sialic acid.
To identify a determinant of human H3 hemagglutinin (HA) amino acid residues linked to the recognition of molecular species of sialic acid, we generated six mutant viruses possessing either the wild-type HA gene from A/Memphis/1/71 (H3N2) or a genetically single-mutated HA gene at position 137, 144, 155, 158 or 193 from a genetic backbone of A/WSN/33 (H1N1) by reverse genetics. We evaluated the binding ability with four types of synthetic sialylglycolipids. The results indicate that the amino acid substitutions Thr155 to Tyr and Glu158 to Gly in H3 HA facilitate virus binding to N-glycolylneuraminic acid.
Takahashi
Tadanobu
T
Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, Shizuoka 422-8526, Japan.
Hashimoto
Asako
A
Maruyama
Mami
M
Ishida
Hideharu
H
Kiso
Makoto
M
Kawaoka
Yoshihiro
Y
Suzuki
Yasuo
Y
Suzuki
Takashi
T
D000595:Amino Acid Sequence; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D053122:Influenza A Virus, H3N2 Subtype / Q000378:metabolism*; D009154:Mutation; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D011487:Protein Conformation
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D019158:N-Acetylneuraminic Acid