Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049647 | FEBS Letters | 2009 | 4 Pages |
Abstract
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.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Tadanobu Takahashi, Asako Hashimoto, Mami Maruyama, Hideharu Ishida, Makoto Kiso, Yoshihiro Kawaoka, Yasuo Suzuki, Takashi Suzuki,